1a6x: Difference between revisions

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[[Image:1a6x.gif|left|200px]]
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[[Image:1a6x.png|left|200px]]


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{{STRUCTURE_1a6x|  PDB=1a6x  |  SCENE=  }}  
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'''STRUCTURE OF THE APO-BIOTIN CARBOXYL CARRIER PROTEIN (APO-BCCP87) OF ESCHERICHIA COLI ACETYL-COA CARBOXYLASE, NMR, 49 STRUCTURES'''
===STRUCTURE OF THE APO-BIOTIN CARBOXYL CARRIER PROTEIN (APO-BCCP87) OF ESCHERICHIA COLI ACETYL-COA CARBOXYLASE, NMR, 49 STRUCTURES===




==Overview==
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The biotin carboxyl carrier protein (BCCP) is a subunit of acetyl-CoA carboxylase, a biotin-dependent enzyme that catalyzes the first committed step of fatty acid biosynthesis. In its functional cycle the biotin carboxyl carrier protein engages in heterologous protein-protein interactions with three distinct partners, depending on its state of posttranslational modification. Apo-BCCP interacts specifically with the biotin holoenzyme synthetase, BirA, which results in the posttranslational attachment of biotin to an essential lysine residue on BCCP. Holo-BCCP then interacts with the biotin carboxylase subunit, which leads to the addition of the carboxylate group of bicarbonate to biotin. Finally, the carboxybiotinylated form of BCCP interacts with transcarboxylase in the conversion of acetyl-CoA to malonyl-CoA. The determinants of protein-protein interaction specificity in this system are unknown. One hypothesis is that posttranslational modification of BCCP may result in conformational changes that regulate specific protein-protein interactions. To test this hypothesis, we have determined the NMR solution structure of the unbiotinylated form of an 87 residue C-terminal domain fragment of BCCP (apoBCCP87) from Escherichia coli acetyl-CoA carboxylase and compared this structure with the high-resolution structure of the biotinylated form that was recently solved by X-ray crystallographic techniques. Although the overall folding of the two proteins is highly similar, small structural differences are apparent for residues of the biotin-binding loop that may be important for mediating specific protein-protein interactions.
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{{ABSTRACT_PUBMED_9398236}}


==About this Structure==
==About this Structure==
1A6X 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=1A6X OCA].  
1A6X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A6X OCA].  


==Reference==
==Reference==
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[[Category: Biotin carboxyl carrier protein]]
[[Category: Biotin carboxyl carrier protein]]
[[Category: Nuclear magnetic resonance]]
[[Category: Nuclear magnetic resonance]]
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Revision as of 13:16, 30 June 2008

File:1a6x.png

Template:STRUCTURE 1a6x

STRUCTURE OF THE APO-BIOTIN CARBOXYL CARRIER PROTEIN (APO-BCCP87) OF ESCHERICHIA COLI ACETYL-COA CARBOXYLASE, NMR, 49 STRUCTURES

Template:ABSTRACT PUBMED 9398236

About this Structure

1A6X is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

Reference

Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase., Yao X, Wei D, Soden C Jr, Summers MF, Beckett D, Biochemistry. 1997 Dec 9;36(49):15089-100. PMID:9398236

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