2pnf

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==Overview==
==Overview==
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The gene product of fabG from Aquifex aeolicus has been heterologously, expressed in Escherichia coli. Purification of the protein took place, using anion-exchange and size-exclusion chromatography and the protein was, then crystallized. Diffraction data were collected to a maximum resolution, of 1.8 A and the initial phases were determined by molecular replacement., The A. aeolicus FabG protein is a putative beta-ketoacyl-acyl carrier, protein reductase. Structure-function studies of this protein are being, performed as part of a larger project investigating naturally occurring, deviations from highly conserved residues within the short-chain, oxidoreductase (SCOR) family.
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The gene product of fabG from Aquifex aeolicus has been heterologously expressed in Escherichia coli. Purification of the protein took place using anion-exchange and size-exclusion chromatography and the protein was then crystallized. Diffraction data were collected to a maximum resolution of 1.8 A and the initial phases were determined by molecular replacement. The A. aeolicus FabG protein is a putative beta-ketoacyl-acyl carrier protein reductase. Structure-function studies of this protein are being performed as part of a larger project investigating naturally occurring deviations from highly conserved residues within the short-chain oxidoreductase (SCOR) family.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Mao, Q.]]
[[Category: Mao, Q.]]
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[[Category: Umland, T.C.]]
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[[Category: Umland, T C.]]
[[Category: 1PE]]
[[Category: 1PE]]
[[Category: MES]]
[[Category: MES]]
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[[Category: short chain oxidoreductase]]
[[Category: short chain oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:29:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:31:17 2008''

Revision as of 16:31, 21 February 2008


2pnf, resolution 1.80Å

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Structure of Aquifex Aeolicus FabG 3-oxoacyl-(acyl-carrier protein) reductase

Overview

The gene product of fabG from Aquifex aeolicus has been heterologously expressed in Escherichia coli. Purification of the protein took place using anion-exchange and size-exclusion chromatography and the protein was then crystallized. Diffraction data were collected to a maximum resolution of 1.8 A and the initial phases were determined by molecular replacement. The A. aeolicus FabG protein is a putative beta-ketoacyl-acyl carrier protein reductase. Structure-function studies of this protein are being performed as part of a larger project investigating naturally occurring deviations from highly conserved residues within the short-chain oxidoreductase (SCOR) family.

About this Structure

2PNF is a Single protein structure of sequence from Aquifex aeolicus with and as ligands. Active as [acyl-carrier-protein_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number 1.1.1.100 Full crystallographic information is available from OCA.

Reference

Crystallization and X-ray diffraction analysis of the beta-ketoacyl-acyl carrier protein reductase FabG from Aquifex aeolicus VF5., Mao Q, Duax WL, Umland TC, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Feb 1;63(Pt, 2):106-9. Epub 2007 Jan 17. PMID:17277451 [[Category: 3-oxoacyl-[acyl-carrier-protein] reductase]]

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