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2bix

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Revision as of 07:58, 19 February 2020

Crystal structure of apocarotenoid cleavage oxygenase from Synechocystis, Fe-free apoenzyme

Structural highlights

2bix is a 2 chain structure with sequence from Aphanocapsa sp. (strain n-1). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2biw
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ACOX_SYNY3] Cleaves a number of carotenals and carotenols in the all-trans configuration at the 15-15' double bond producing retinal or retinol, respectively. Also shows activity toward lycopenals and the corresponding alcohols. Does not cleave beta-carotene or lycopene.

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

Enzymes that produce retinal and related apocarotenoids constitute a sequence- and thus structure-related family, a member of which was analyzed by x-ray diffraction. This member is an oxygenase and contains an Fe2+-4-His arrangement at the axis of a seven-bladed beta-propeller chain fold covered by a dome formed by six large loops. The Fe2+ is accessible through a long nonpolar tunnel that holds a carotenoid derivative in one of the crystals. On binding, three consecutive double bonds of this carotenoid changed from a straight all-trans to a cranked cis-trans-cis conformation. The remaining trans bond is located at the dioxygen-ligated Fe2+ and cleaved by oxygen.

The structure of a retinal-forming carotenoid oxygenase.,Kloer DP, Ruch S, Al-Babili S, Beyer P, Schulz GE Science. 2005 Apr 8;308(5719):267-9. PMID:15821095^[1]

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

References

↑ Kloer DP, Ruch S, Al-Babili S, Beyer P, Schulz GE. The structure of a retinal-forming carotenoid oxygenase. Science. 2005 Apr 8;308(5719):267-9. PMID:15821095 doi:308/5719/267

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bix"

@@ Line 1: / Line 1: @@
 ==Crystal structure of apocarotenoid cleavage oxygenase from Synechocystis, Fe-free apoenzyme==
-<StructureSection load='2bix' size='340' side='right' caption='[[2bix]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
+<StructureSection load='2bix' size='340' side='right'caption='[[2bix]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2bix]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BIX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BIX FirstGlance]. <br>
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Al-Babili, S]]
 [[Category: Beyer, P]]

2bix

From Proteopedia

Revision as of 07:58, 19 February 2020

Crystal structure of apocarotenoid cleavage oxygenase from Synechocystis, Fe-free apoenzyme

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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