4cfs

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{{STRUCTURE_4cfs| PDB=4cfs | SCENE= }}
{{STRUCTURE_4cfs| PDB=4cfs | SCENE= }}
===CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4- OXOQUINALDINE 2,4-DIOXYGENASE (HOD) CATALYTICALLY INACTIVE H251A VARIANT COMPLEXED WITH ITS NATURAL SUBSTRATE 1-H-3-HYDROXY-4- OXOQUINALDINE===
===CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4- OXOQUINALDINE 2,4-DIOXYGENASE (HOD) CATALYTICALLY INACTIVE H251A VARIANT COMPLEXED WITH ITS NATURAL SUBSTRATE 1-H-3-HYDROXY-4- OXOQUINALDINE===
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{{ABSTRACT_PUBMED_20080731}}
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{{ABSTRACT_PUBMED_24482238}}
==Function==
==Function==
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==About this Structure==
==About this Structure==
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[[4cfs]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CFS OCA].
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[[4cfs]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Artnt Artnt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CFS OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:020080731</ref><references group="xtra"/><references/>
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<ref group="xtra">PMID:024482238</ref><references group="xtra"/><references/>
[[Category: 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase]]
[[Category: 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase]]
 +
[[Category: Artnt]]
[[Category: Bui, S.]]
[[Category: Bui, S.]]
[[Category: Steiner, R A.]]
[[Category: Steiner, R A.]]

Revision as of 03:31, 13 February 2014

Template:STRUCTURE 4cfs

Contents

CRYSTAL STRUCTURE OF THE COFACTOR-DEVOID 1-H-3-HYDROXY-4- OXOQUINALDINE 2,4-DIOXYGENASE (HOD) CATALYTICALLY INACTIVE H251A VARIANT COMPLEXED WITH ITS NATURAL SUBSTRATE 1-H-3-HYDROXY-4- OXOQUINALDINE

Template:ABSTRACT PUBMED 24482238

Function

[HOD_ARTNT] Ring-cleaving dioxygenase involved in quinaldine degradation and utilization.[1]

About this Structure

4cfs is a 4 chain structure with sequence from Artnt. Full crystallographic information is available from OCA.

Reference

  • Hernandez-Ortega A, Quesne MG, Bui S, Heuts DP, Steiner RA, Heyes DJ, de Visser SP, Scrutton NS. Origin of the proton-transfer step in the cofactor-free 1-H-3-hydroxy-4-oxoquinaldine 2,4- dioxygenase: Effect of the basicity of an active site His residue. J Biol Chem. 2014 Jan 30. PMID:24482238 doi:http://dx.doi.org/10.1074/jbc.M113.543033
  1. Betz A, Facey SJ, Hauer B, Tshisuaka B, Lingens F. Molecular cloning, sequencing, expression, and site-directed mutagenesis of the 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase gene from Arthrobacter spec. Ru61a. J Basic Microbiol. 2000;40(1):7-23. PMID:10746195

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