Crystal structures of the methane monooxygenase hydroxylase from <i>Methylococcus capsulatus</i> (Bath): implications for substrate gating and component interactions. Rosenzweig, A. C., Brandstetter, H., Whittington, D. A., Nordlund, P., Lippard, S. J., & Frederick, C. A. Proteins, 29(2):141–152, Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA., 10, 1997. ![Crystal structures of the methane monooxygenase hydroxylase from <i>Methylococcus capsulatus</i> (Bath): implications for substrate gating and component interactions. [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper abstract bibtex The crystal structure of the nonheme iron-containing hydroxylase component of methane monooxygenase hydroxylase (MMOH) from Methylococcus capsulatus (Bath) has been solved in two crystal forms, one of which was refined to 1.7 A resolution. The enzyme is composed of two copies each of three subunits (alpha 2 beta 2 gamma 2), and all three subunits are almost completely alpha-helical, with the exception of two beta hairpin structures in the alpha subunit. The active site of each alpha subunit contains one dinuclear iron center, housed in a four-helix bundle. The two iron atoms are octahedrally coordinated by 2 histidine and 4 glutamic acid residues as well as by a bridging hydroxide ion, a terminal water molecule, and at 4 degrees C, a bridging acetate ion, which is replaced at -160 degrees C with a bridging water molecule. Comparison of the results for two crystal forms demonstrates overall conservation and relative orientation of the domain structures. The most prominent structural differences identified between the two crystal forms is in an altered side chain conformation for Leu 110 at the active site cavity. We suggest that this residue serves as one component of a hydrophobic gate controlling access of substrates to and products from the active site. The leucine gate may be responsible for the effect of the B protein component on the reactivity of the reduced hydroxylase with dioxygen. A potential reductase binding site has been assigned based on an analysis of crystal packing in the two forms and corroborated by inhibition studies with a synthetic peptide corresponding to the proposed docking position.
@article{citeulike:1079825,
abstract = {The crystal structure of the nonheme iron-containing hydroxylase component
of methane monooxygenase hydroxylase (MMOH) from Methylococcus capsulatus
(Bath) has been solved in two crystal forms, one of which was refined
to 1.7 A resolution. The enzyme is composed of two copies each of
three subunits (alpha 2 beta 2 gamma 2), and all three subunits
are almost completely alpha-helical, with the exception of two beta
hairpin structures in the alpha subunit. The active site of each
alpha subunit contains one dinuclear iron center, housed in a four-helix
bundle. The two iron atoms are octahedrally coordinated by 2 histidine
and 4 glutamic acid residues as well as by a bridging hydroxide
ion, a terminal water molecule, and at 4 degrees C, a bridging acetate
ion, which is replaced at -160 degrees C with a bridging water molecule.
Comparison of the results for two crystal forms demonstrates overall
conservation and relative orientation of the domain structures.
The most prominent structural differences identified between the
two crystal forms is in an altered side chain conformation for Leu
110 at the active site cavity. We suggest that this residue serves
as one component of a hydrophobic gate controlling access of substrates
to and products from the active site. The leucine gate may be responsible
for the effect of the B protein component on the reactivity of the
reduced hydroxylase with dioxygen. A potential reductase binding
site has been assigned based on an analysis of crystal packing in
the two forms and corroborated by inhibition studies with a synthetic
peptide corresponding to the proposed docking position.},
added-at = {2007-02-02T11:54:15.000+0100},
address = {Department of Biological Chemistry and Molecular Pharmacology, Harvard
Medical School, Boston, MA 02115, USA.},
author = {Rosenzweig, A. C. and Brandstetter, H. and Whittington, D. A. and Nordlund, P. and Lippard, S. J. and Frederick, C. A.},
biburl = {https://www.bibsonomy.org/bibtex/29377ca76e75ef99fab5c0c4d0aca76a8/robert},
citeulike-article-id = {1079825},
interhash = {f0b2fa2d05c2fad3e4f2ef52b30cf03a},
intrahash = {9377ca76e75ef99fab5c0c4d0aca76a8},
issn = {0887-3585},
journal = {Proteins},
keywords = {crystal-structure},
month = {10},
number = 2,
pages = {141--152},
priority = {2},
timestamp = {2007-02-02T11:54:15.000+0100},
title = {Crystal structures of the methane monooxygenase hydroxylase from
\textit{Methylococcus capsulatus} (Bath): implications for substrate
gating and component interactions.},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=9329079},
volume = 29,
year = 1997
}
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The active site of each alpha subunit contains one dinuclear iron center, housed in a four-helix bundle. The two iron atoms are octahedrally coordinated by 2 histidine and 4 glutamic acid residues as well as by a bridging hydroxide ion, a terminal water molecule, and at 4 degrees C, a bridging acetate ion, which is replaced at -160 degrees C with a bridging water molecule. Comparison of the results for two crystal forms demonstrates overall conservation and relative orientation of the domain structures. The most prominent structural differences identified between the two crystal forms is in an altered side chain conformation for Leu 110 at the active site cavity. We suggest that this residue serves as one component of a hydrophobic gate controlling access of substrates to and products from the active site. The leucine gate may be responsible for the effect of the B protein component on the reactivity of the reduced hydroxylase with dioxygen. 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The enzyme is composed of two copies each of\r\n\tthree subunits (alpha 2 beta 2 gamma 2), and all three subunits\r\n\tare almost completely alpha-helical, with the exception of two beta\r\n\thairpin structures in the alpha subunit. The active site of each\r\n\talpha subunit contains one dinuclear iron center, housed in a four-helix\r\n\tbundle. The two iron atoms are octahedrally coordinated by 2 histidine\r\n\tand 4 glutamic acid residues as well as by a bridging hydroxide\r\n\tion, a terminal water molecule, and at 4 degrees C, a bridging acetate\r\n\tion, which is replaced at -160 degrees C with a bridging water molecule.\r\n\tComparison of the results for two crystal forms demonstrates overall\r\n\tconservation and relative orientation of the domain structures.\r\n\tThe most prominent structural differences identified between the\r\n\ttwo crystal forms is in an altered side chain conformation for Leu\r\n\t110 at the active site cavity. We suggest that this residue serves\r\n\tas one component of a hydrophobic gate controlling access of substrates\r\n\tto and products from the active site. The leucine gate may be responsible\r\n\tfor the effect of the B protein component on the reactivity of the\r\n\treduced hydroxylase with dioxygen. A potential reductase binding\r\n\tsite has been assigned based on an analysis of crystal packing in\r\n\tthe two forms and corroborated by inhibition studies with a synthetic\r\n\tpeptide corresponding to the proposed docking position.},\n added-at = {2007-02-02T11:54:15.000+0100},\n address = {Department of Biological Chemistry and Molecular Pharmacology, Harvard\r\n\tMedical School, Boston, MA 02115, USA.},\n author = {Rosenzweig, A. C. and Brandstetter, H. and Whittington, D. A. and Nordlund, P. and Lippard, S. J. and Frederick, C. 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