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4l9z

From Proteopedia

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'''Unreleased structure'''
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{{STRUCTURE_4l9z| PDB=4l9z | SCENE= }}
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===Crystal Structure of Rhodobacter sphaeroides malyl-CoA lyase in complex with magnesium, oxalate, and CoA===
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{{ABSTRACT_PUBMED_24206647}}
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The entry 4l9z is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/MCAL_RHOS4 MCAL_RHOS4]] Catalyzes the reversible condensation of glyoxylate and acetyl-CoA to L-malyl-CoA and the reversible condensation of glyoxylate and propionyl-CoA to beta-methylmalyl-CoA.<ref>PMID:20047909</ref>
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Authors: Zarzycki, J., Kerfeld, C.A.
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==About this Structure==
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[[4l9z]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L9Z OCA].
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Description: Crystal Structure of Rhodobacter sphaeroides malyl-CoA lyase in complex with magnesium, oxalate, and CoA
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==Reference==
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<ref group="xtra">PMID:024206647</ref><references group="xtra"/><references/>
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[[Category: Malyl-CoA lyase]]
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[[Category: Kerfeld, C A.]]
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[[Category: Zarzycki, J.]]
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[[Category: Lyase]]
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[[Category: Tim barrel]]

Revision as of 07:24, 4 December 2013

Template:STRUCTURE 4l9z

Contents

Crystal Structure of Rhodobacter sphaeroides malyl-CoA lyase in complex with magnesium, oxalate, and CoA

Template:ABSTRACT PUBMED 24206647

Function

[MCAL_RHOS4] Catalyzes the reversible condensation of glyoxylate and acetyl-CoA to L-malyl-CoA and the reversible condensation of glyoxylate and propionyl-CoA to beta-methylmalyl-CoA.[1]

About this Structure

4l9z is a 6 chain structure. Full crystallographic information is available from OCA.

Reference

  • Zarzycki J, Kerfeld CA. The crystal structures of the tri-functional Chloroflexus aurantiacus and bi-functional Rhodobacter sphaeroides malyl-CoA lyases and comparison with CitE-like superfamily enzymes and malate synthases. BMC Struct Biol. 2013 Nov 9;13(1):28. PMID:24206647 doi:http://dx.doi.org/10.1186/1472-6807-13-28
  1. Erb TJ, Frerichs-Revermann L, Fuchs G, Alber BE. The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-Malyl-coenzyme A (CoA)/{beta}-methylmalyl-CoA lyase and (3S)- Malyl-CoA thioesterase. J Bacteriol. 2010 Mar;192(5):1249-58. doi: 10.1128/JB.01267-09. Epub 2010 Jan 4. PMID:20047909 doi:http://dx.doi.org/10.1128/JB.01267-09

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