1ckv

From Proteopedia

(Difference between revisions)

Revision as of 10:37, 14 July 2021

STRUCTURE OF THE SOLUBLE METHANE MONOOXYGENASE REGULATORY PROTEIN B

Structural highlights

1ckv is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MMOB_METCA] The B protein acts as a regulator of electron flow through the soluble mmo complex, switching the enzyme from an oxidase to a hydroxylase in the presence of the substrate.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The soluble methane monooxygenase (sMMO; EC 1.14.13.25) from the pseudothermophile Methylococcus capsulatus (Bath) is a three-component enzyme system that catalyzes the selective oxidation of methane to methanol. We have used NMR spectroscopy to produce a highly refined structure of MMOB, the 16-kDa regulatory protein of this system. This structure has a unique and intricate fold containing seven beta-strands forming two beta-sheets oriented perpendicular to each other and bridged by three alpha-helices. The rate and efficiency of the methane hydroxylation by sMMO depend on dynamic binding interactions of the hydroxylase with the reductase and regulatory protein components during catalysis. We have monitored by NMR the binding of MMOB to the hydroxylase in the presence and absence of the reductase. The results of these studies provide structural insight into how the regulatory protein interacts with the hydroxylase.

Structure of the soluble methane monooxygenase regulatory protein B.,Walters KJ, Gassner GT, Lippard SJ, Wagner G Proc Natl Acad Sci U S A. 1999 Jul 6;96(14):7877-82. PMID:10393915^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Walters KJ, Gassner GT, Lippard SJ, Wagner G. Structure of the soluble methane monooxygenase regulatory protein B. Proc Natl Acad Sci U S A. 1999 Jul 6;96(14):7877-82. PMID:10393915

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ckv"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ckv' size='340' side='right'caption='[[1ckv]], [[NMR_Ensembles_of_Models | 14 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ckv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CKV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CKV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ckv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CKV FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ckv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ckv OCA], [http://pdbe.org/1ckv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ckv RCSB], [http://www.ebi.ac.uk/pdbsum/1ckv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ckv ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ckv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ckv OCA], [https://pdbe.org/1ckv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ckv RCSB], [https://www.ebi.ac.uk/pdbsum/1ckv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ckv ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MMOB_METCA MMOB_METCA]] The B protein acts as a regulator of electron flow through the soluble mmo complex, switching the enzyme from an oxidase to a hydroxylase in the presence of the substrate.
+[[https://www.uniprot.org/uniprot/MMOB_METCA MMOB_METCA]] The B protein acts as a regulator of electron flow through the soluble mmo complex, switching the enzyme from an oxidase to a hydroxylase in the presence of the substrate.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 27: / Line 27: @@
 </div>
 <div class="pdbe-citations 1ckv" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Methane monooxygenase|Methane monooxygenase]]
 == References ==
 <references/>

1ckv

From Proteopedia

Revision as of 10:37, 14 July 2021

STRUCTURE OF THE SOLUBLE METHANE MONOOXYGENASE REGULATORY PROTEIN B

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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