1dv2

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{{STRUCTURE_1dv2| PDB=1dv2 | SCENE= }}
{{STRUCTURE_1dv2| PDB=1dv2 | SCENE= }}
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'''The structure of biotin carboxylase, mutant E288K, complexed with ATP'''
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===The structure of biotin carboxylase, mutant E288K, complexed with ATP===
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==Overview==
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Acetyl-CoA carboxylase catalyzes the first committed step in fatty acid synthesis. In Escherichia coli, the enzyme is composed of three distinct protein components: biotin carboxylase, biotin carboxyl carrier protein, and carboxyltransferase. The biotin carboxylase component has served for many years as a paradigm for mechanistic studies devoted toward understanding more complicated biotin-dependent carboxylases. The three-dimensional x-ray structure of an unliganded form of E. coli biotin carboxylase was originally solved in 1994 to 2.4-A resolution. This study revealed the architecture of the enzyme and demonstrated that the protein belongs to the ATP-grasp superfamily. Here we describe the three-dimensional structure of the E. coli biotin carboxylase complexed with ATP and determined to 2.5-A resolution. The major conformational change that occurs upon nucleotide binding is a rotation of approximately 45(o) of one domain relative to the other domains thereby closing off the active site pocket. Key residues involved in binding the nucleotide to the protein include Lys-116, His-236, and Glu-201. The backbone amide groups of Gly-165 and Gly-166 participate in hydrogen bonding interactions with the phosphoryl oxygens of the nucleotide. A comparison of this closed form of biotin carboxylase with carbamoyl-phosphate synthetase is presented.
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(as it appears on PubMed at http://www.pubmed.gov), where 10821865 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10821865}}
==About this Structure==
==About this Structure==
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[[Category: Waldrop, G L.]]
[[Category: Waldrop, G L.]]
[[Category: Atp-grasp biotin-dependent carboxylase]]
[[Category: Atp-grasp biotin-dependent carboxylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:18:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:39:36 2008''

Revision as of 20:39, 30 June 2008

Image:1dv2.png

Template:STRUCTURE 1dv2

The structure of biotin carboxylase, mutant E288K, complexed with ATP

Template:ABSTRACT PUBMED 10821865

About this Structure

1DV2 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Movement of the biotin carboxylase B-domain as a result of ATP binding., Thoden JB, Blanchard CZ, Holden HM, Waldrop GL, J Biol Chem. 2000 May 26;275(21):16183-90. PMID:10821865

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