1dv2
From Proteopedia
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| - | [[Image:1dv2.jpg|left|200px]] | + | [[Image:1dv2.jpg|left|200px]] |
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| - | '''The structure of biotin carboxylase, mutant E288K, complexed with ATP''' | + | {{Structure |
| + | |PDB= 1dv2 |SIZE=350|CAPTION= <scene name='initialview01'>1dv2</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Biotin_carboxylase Biotin carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.14 6.3.4.14] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''The structure of biotin carboxylase, mutant E288K, complexed with ATP''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DV2 is a [ | + | 1DV2 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=1DV2 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10821865 10821865] |
[[Category: Biotin carboxylase]] | [[Category: Biotin carboxylase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: atp-grasp biotin-dependent carboxylase]] | [[Category: atp-grasp biotin-dependent carboxylase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:44:48 2008'' |
Revision as of 08:44, 20 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Biotin carboxylase, with EC number 6.3.4.14 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The structure of biotin carboxylase, mutant E288K, complexed with ATP
Overview
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.
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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