1wnd
From Proteopedia
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- | [[Image:1wnd.gif|left|200px]] | + | [[Image:1wnd.gif|left|200px]] |
- | + | ||
- | '''Escherichia coli YdcW gene product is a medium-chain aldehyde dehydrogenase as determined by kinetics and crystal stucture''' | + | {{Structure |
+ | |PDB= 1wnd |SIZE=350|CAPTION= <scene name='initialview01'>1wnd</scene>, resolution 2.10Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Betaine-aldehyde_dehydrogenase Betaine-aldehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.8 1.2.1.8] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Escherichia coli YdcW gene product is a medium-chain aldehyde dehydrogenase as determined by kinetics and crystal stucture''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1WND is a [ | + | 1WND is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WND OCA]. |
==Reference== | ==Reference== | ||
- | Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase., Gruez A, Roig-Zamboni V, Grisel S, Salomoni A, Valencia C, Campanacci V, Tegoni M, Cambillau C, J Mol Biol. 2004 Oct 8;343(1):29-41. PMID:[http:// | + | Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase., Gruez A, Roig-Zamboni V, Grisel S, Salomoni A, Valencia C, Campanacci V, Tegoni M, Cambillau C, J Mol Biol. 2004 Oct 8;343(1):29-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15381418 15381418] |
[[Category: Betaine-aldehyde dehydrogenase]] | [[Category: Betaine-aldehyde dehydrogenase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: crystal structure]] | [[Category: crystal structure]] | ||
[[Category: fluorescence]] | [[Category: fluorescence]] | ||
- | [[Category: | + | [[Category: kinetic]] |
[[Category: nadh]] | [[Category: nadh]] | ||
- | ''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 14:59:16 2008'' |
Revision as of 12:59, 20 March 2008
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, resolution 2.10Å | |||||||
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Ligands: | |||||||
Activity: | Betaine-aldehyde dehydrogenase, with EC number 1.2.1.8 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Escherichia coli YdcW gene product is a medium-chain aldehyde dehydrogenase as determined by kinetics and crystal stucture
Overview
In the context of a medium-scaled structural genomics program aiming at solving the structures of as many as possible bacterial unknown open reading frame products from Escherichia coli (Y prefix), we have solved the structure of YdcW at 2.1A resolution, using molecular replacement. According to its sequence identity, YdcW has been classified into the betaine aldehyde dehydrogenases family (EC 1.2.1.8), catalysing the oxidation of betaine aldehyde into glycine betaine. The structure of YdcW resembles that of other aldehyde dehydrogenases: it is tetrameric and binds a NADH molecule in each monomer. The NADH molecules, bound in the active site by soaking, are revealed to be in the "hydrolysis position". Activities experiments demonstrate that YdcW is more active on medium-chains aldehyde than on betaine aldehyde. However, soaking of betaine into YdcW crystals revealed its presence in one of the subunits, in two positions, a putative resting position and a hydride transfer ready position. Analysis of kinetics data and of the active site shape suggest an optimum binding of n-alkyl aldehydes up to seven to eight carbon atoms, possibly followed by a bulky cyclic or aromatic group.
About this Structure
1WND is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase., Gruez A, Roig-Zamboni V, Grisel S, Salomoni A, Valencia C, Campanacci V, Tegoni M, Cambillau C, J Mol Biol. 2004 Oct 8;343(1):29-41. PMID:15381418
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