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1bdo

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{{STRUCTURE_1bdo| PDB=1bdo | SCENE= }}
{{STRUCTURE_1bdo| PDB=1bdo | SCENE= }}
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'''STRUCTURE OF THE BIOTINYL DOMAIN OF ACETYL-COENZYME A CARBOXYLASE DETERMINED BY MAD PHASING'''
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===STRUCTURE OF THE BIOTINYL DOMAIN OF ACETYL-COENZYME A CARBOXYLASE DETERMINED BY MAD PHASING===
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==Overview==
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BACKGROUND: Acetyl-coenzyme A carboxylase catalyzes the first committed step of fatty acid biosynthesis. Universally, this reaction involves three functional components all related to a carboxybiotinyl intermediate. A biotinyl domain shuttles its covalently attached biotin prosthetic group between the active sites of a biotin carboxylase and a carboxyl transferase. In Escherichia coli, the three components reside in separate subunits: a biotinyl domain is the functional portion of one of these, biotin carboxy carrier protein (BCCP). RESULTS: We have expressed natural and selenomethionyl (Se-met) BCCP from E. coli as biotinylated recombinant proteins, proteolyzed them with subtilisin Carlsberg to produce the biotinyl domains BCCP and Se-met BCCPsc, determined the crystal structure of Se-met BCCPsc using a modified version of the multiwavelength anomalous diffraction (MAD) phasing protocol, and refined the structure for the natural BCCPsc at 1.8 A resolution. The structure may be described as a capped beta sandwich with quasi-dyad symmetry. Each half contains a characteristic hammerhead motif. The biotinylated lysin is located at a hairpin beta turn which connects the two symmetric halves of the molecule, and its biotinyl group interacts with a non-symmetric protrusion from the core. CONCLUSIONS: This first crystal structure of a biotinyl domain helps to unravel the central role of such domains in reactions catalyzed by biotin-dependent carboxylases. The hammerhead structure observed twice in BCCPsc may be regarded as the basic structural motif of biotinyl and lipoyl domains of a superfamily of enzymes. The new MAD phasing techniques developed in the course of determining this structure enhance the power of the MAD method.
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==About this Structure==
==About this Structure==
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[[Category: Ligase]]
[[Category: Ligase]]
[[Category: Selenomethionine]]
[[Category: Selenomethionine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:22:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:54:52 2008''

Revision as of 15:54, 30 June 2008

Image:1bdo.png

Template:STRUCTURE 1bdo

STRUCTURE OF THE BIOTINYL DOMAIN OF ACETYL-COENZYME A CARBOXYLASE DETERMINED BY MAD PHASING

Template:ABSTRACT PUBMED 8747466

About this Structure

1BDO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing., Athappilly FK, Hendrickson WA, Structure. 1995 Dec 15;3(12):1407-19. PMID:8747466

Page seeded by OCA on Mon Jun 30 18:54:52 2008

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