1xvg: Difference between revisions
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[[Image:1xvg.gif|left|200px]] | [[Image:1xvg.gif|left|200px]] | ||
'''soluble methane monooxygenase hydroxylase: bromoethanol soaked structure''' | {{Structure | ||
|PDB= 1xvg |SIZE=350|CAPTION= <scene name='initialview01'>1xvg</scene>, resolution 1.96Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=BRJ:2-BROMOETHANOL'>BRJ</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Methane_monooxygenase Methane monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.25 1.14.13.25] | |||
|GENE= | |||
}} | |||
'''soluble methane monooxygenase hydroxylase: bromoethanol soaked structure''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1XVG is a [ | 1XVG is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XVG OCA]. | ||
==Reference== | ==Reference== | ||
Product bound structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): protein motion in the alpha-subunit., Sazinsky MH, Lippard SJ, J Am Chem Soc. 2005 Apr 27;127(16):5814-25. PMID:[http:// | Product bound structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): protein motion in the alpha-subunit., Sazinsky MH, Lippard SJ, J Am Chem Soc. 2005 Apr 27;127(16):5814-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15839679 15839679] | ||
[[Category: Methane monooxygenase]] | [[Category: Methane monooxygenase]] | ||
[[Category: Methylococcus capsulatus]] | [[Category: Methylococcus capsulatus]] | ||
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[[Category: CA]] | [[Category: CA]] | ||
[[Category: FE]] | [[Category: FE]] | ||
[[Category: | [[Category: cavity]] | ||
[[Category: diiron]] | [[Category: diiron]] | ||
[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
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[[Category: product binding]] | [[Category: product binding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:15:03 2008'' | ||
Revision as of 16:15, 20 March 2008
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| , resolution 1.96Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | Methane monooxygenase, with EC number 1.14.13.25 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
soluble methane monooxygenase hydroxylase: bromoethanol soaked structure
OverviewOverview
The soluble methane monooxygenase hydroxylase (MMOH) alpha-subunit contains a series of cavities that delineate the route of substrate entrance to and product egress from the buried carboxylate-bridged diiron center. The presence of discrete cavities is a major structural difference between MMOH, which can hydroxylate methane, and toluene/o-xylene monooxygenase hydroxylase (ToMOH), which cannot. To understand better the functions of the cavities and to investigate how an enzyme designed for methane hydroxylation can also accommodate larger substrates such as octane, methylcubane, and trans-1-methyl-2-phenylcyclopropane, MMOH crystals were soaked with an assortment of different alcohols and their X-ray structures were solved to 1.8-2.4 A resolution. The product analogues localize to cavities 1-3 and delineate a path of product exit and/or substrate entrance from the active site to the surface of the protein. The binding of the alcohols to a position bridging the two iron atoms in cavity 1 extends and validates previous crystallographic, spectroscopic, and computational work indicating this site to be where substrates are hydroxylated and products form. The presence of these alcohols induces perturbations in the amino acid side-chain gates linking pairs of cavities, allowing for the formation of a channel similar to one observed in ToMOH. Upon binding of 6-bromohexan-1-ol, the pi helix formed by residues 202-211 in helix E of the alpha-subunit is extended through residue 216, changing the orientations of several amino acid residues in the active site cavity. This remarkable secondary structure rearrangement in the four-helix bundle has several mechanistic implications for substrate accommodation and the function of the effector protein, MMOB.
About this StructureAbout this Structure
1XVG is a Protein complex structure of sequences from Methylococcus capsulatus. Full crystallographic information is available from OCA.
ReferenceReference
Product bound structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): protein motion in the alpha-subunit., Sazinsky MH, Lippard SJ, J Am Chem Soc. 2005 Apr 27;127(16):5814-25. PMID:15839679
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