2bdo

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[[Image:2bdo.gif|left|200px]]
[[Image:2bdo.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2bdo |SIZE=350|CAPTION= <scene name='initialview01'>2bdo</scene>
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The line below this paragraph, containing "STRUCTURE_2bdo", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=BTN:BIOTIN'>BTN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase Acetyl-CoA carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2] </span>
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{{STRUCTURE_2bdo| PDB=2bdo | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bdo OCA], [http://www.ebi.ac.uk/pdbsum/2bdo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bdo RCSB]</span>
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'''SOLUTION STRUCTURE OF HOLO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY'''
'''SOLUTION STRUCTURE OF HOLO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY'''
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[[Category: Shu, N.]]
[[Category: Shu, N.]]
[[Category: Wallace, J C.]]
[[Category: Wallace, J C.]]
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[[Category: acetyl coa carboxylase]]
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[[Category: Acetyl coa carboxylase]]
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[[Category: biotin]]
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[[Category: Biotin]]
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[[Category: biotinyl domain]]
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[[Category: Biotinyl domain]]
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[[Category: nmr spectroscopy]]
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[[Category: Nmr spectroscopy]]
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[[Category: protein structure]]
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[[Category: Protein structure]]
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[[Category: swinging arm]]
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[[Category: Swinging arm]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:08:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:04:48 2008''
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Revision as of 17:08, 3 May 2008

Template:STRUCTURE 2bdo

SOLUTION STRUCTURE OF HOLO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY


Overview

A subgene encoding the 87 C-terminal amino acids of the biotinyl carboxy carrier protein (BCCP) from the acetyl CoA carboxylase of Escherichia coli was overexpressed and the apoprotein biotinylated in vitro. The structures of both the apo and holo forms of the biotinyl domain were determined by means of multidimensional NMR spectroscopy. That of the holo domain was well-defined, except for the 10 N-terminal residues, which form part of the flexible linker between the biotinyl and subunit-binding domains of BCCP. In agreement with X-ray crystallographic studies [Athappilly, F. K., and Hendrickson, W. A. (1995) Structure 3, 1407-1419], the structure comprises a flattened beta-barrel composed of two four-stranded beta-sheets with a 2-fold axis of quasi-symmetry and the biotinyl-lysine residue displayed in an exposed beta-turn on the side of the protein opposite from the N- and C-terminal residues. The biotin group is immobilized on the protein surface, with the ureido ring held down by interactions with a protruding polypeptide "thumb" formed by residues 94-101. However, at the site of carboxylation, no evidence could be found in solution for the predicted hydrogen bond between the main chain O of Thr94 and the ureido HN1'. The structure of the apo domain is essentially identical, although the packing of side chains is more favorable in the holo domain, and this may be reflected in differences in the dynamics of the two forms. The thumb region appears to be lacking in almost all other biotinyl domain sequences, and it may be that the immobilization of the biotinyl-lysine residue in the biotinyl domain of BCCP is an unusual requirement, needed for the catalytic reaction of acetyl CoA carboxylase.

About this Structure

2BDO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy., Roberts EL, Shu N, Howard MJ, Broadhurst RW, Chapman-Smith A, Wallace JC, Morris T, Cronan JE Jr, Perham RN, Biochemistry. 1999 Apr 20;38(16):5045-53. PMID:10213607 Page seeded by OCA on Sat May 3 20:08:46 2008

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