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2q1u

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{{STRUCTURE_2q1u| PDB=2q1u | SCENE= }}
{{STRUCTURE_2q1u| PDB=2q1u | SCENE= }}
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'''Crystal structure of the Bordetella bronchiseptica enzyme WbmF in complex with NAD+ and UDP'''
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===Crystal structure of the Bordetella bronchiseptica enzyme WbmF in complex with NAD+ and UDP===
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==Overview==
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The pathogenic bacteria Bordetella parapertussis and Bordetella bronchiseptica express a lipopolysaccharide O antigen containing a polymer of 2,3-diacetamido-2,3-dideoxy-l-galacturonic acid. The O-antigen cluster contains three neighbouring genes that encode proteins belonging to the short-chain dehydrogenase/reductase (SDR) family, wbmF, wbmG and wbmH, and we aimed to elucidate their individual functions. Mutation and complementation implicate each gene in O-antigen expression but, as their putative sugar nucleotide substrates are not currently available, biochemical characterisation of WbmF, WbmG and WbmH is impractical at the present time. SDR family members catalyse a wide range of chemical reactions including oxidation, reduction and epimerisation. Because they typically share low sequence conservation, however, catalytic function cannot be predicted from sequence analysis alone. In this context, structural characterisation of the native proteins, co-crystals and small-molecule soaks enables differentiation of the functions of WbmF, WbmG and WbmH. These proteins exhibit typical SDR architecture and coordinate NAD. In the substrate-binding domain, all three enzymes bind uridyl nucleotides. WbmG contains a typical SDR catalytic TYK triad, which is required for oxidoreductase function, but the active site is devoid of additional acid-base functionality. Similarly, WbmH possesses a TYK triad, but an otherwise feature-poor active site. Consequently, 3,5-epimerase function can probably be ruled out for these enzymes. The WbmF active site contains conserved 3,5-epimerase features, namely, a positionally conserved cysteine (Cys133) and basic side chain (His90 or Asn213), but lacks the serine/threonine component of the SDR triad and therefore may not act as an oxidoreductase. The data suggest a pathway for synthesis of the O-antigen precursor UDP-2,3-diacetamido-2,3-dideoxy-l-galacturonic acid and illustrate the usefulness of structural data in predicting protein function.
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(as it appears on PubMed at http://www.pubmed.gov), where 17950751 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17950751}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Predicting protein function from structure--the roles of short-chain dehydrogenase/reductase enzymes in Bordetella O-antigen biosynthesis., King JD, Harmer NJ, Preston A, Palmer CM, Rejzek M, Field RA, Blundell TL, Maskell DJ, J Mol Biol. 2007 Nov 30;374(3):749-63. Epub 2007 Sep 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17950751 17950751]
Predicting protein function from structure--the roles of short-chain dehydrogenase/reductase enzymes in Bordetella O-antigen biosynthesis., King JD, Harmer NJ, Preston A, Palmer CM, Rejzek M, Field RA, Blundell TL, Maskell DJ, J Mol Biol. 2007 Nov 30;374(3):749-63. Epub 2007 Sep 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17950751 17950751]
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Cloning, expression, purification and preliminary crystallographic analysis of the short-chain dehydrogenase enzymes WbmF, WbmG and WbmH from Bordetella bronchiseptica., Harmer NJ, King JD, Palmer CM, Preston A, Maskell DJ, Blundell TL, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt, 8):711-5. Epub 2007 Jul 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17671375 17671375]
[[Category: Bordetella bronchiseptica]]
[[Category: Bordetella bronchiseptica]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Rossman fold]]
[[Category: Rossman fold]]
[[Category: Sugar binding protein]]
[[Category: Sugar binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:11:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:47:17 2008''

Revision as of 10:47, 28 July 2008

Image:2q1u.png

Template:STRUCTURE 2q1u

Crystal structure of the Bordetella bronchiseptica enzyme WbmF in complex with NAD+ and UDP

Template:ABSTRACT PUBMED 17950751

About this Structure

2Q1U is a Single protein structure of sequence from Bordetella bronchiseptica. Full crystallographic information is available from OCA.

Reference

Predicting protein function from structure--the roles of short-chain dehydrogenase/reductase enzymes in Bordetella O-antigen biosynthesis., King JD, Harmer NJ, Preston A, Palmer CM, Rejzek M, Field RA, Blundell TL, Maskell DJ, J Mol Biol. 2007 Nov 30;374(3):749-63. Epub 2007 Sep 26. PMID:17950751

Cloning, expression, purification and preliminary crystallographic analysis of the short-chain dehydrogenase enzymes WbmF, WbmG and WbmH from Bordetella bronchiseptica., Harmer NJ, King JD, Palmer CM, Preston A, Maskell DJ, Blundell TL, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt, 8):711-5. Epub 2007 Jul 28. PMID:17671375

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