1jjv

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(New page: 200px<br /><applet load="1jjv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jjv, resolution 2.&Aring;" /> '''DEPHOSPHO-COA KINASE I...)
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caption="1jjv, resolution 2.&Aring;" />
'''DEPHOSPHO-COA KINASE IN COMPLEX WITH ATP'''<br />
'''DEPHOSPHO-COA KINASE IN COMPLEX WITH ATP'''<br />
==Overview==
==Overview==
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Dephospho-coenzyme A kinase catalyzes the final step in CoA biosynthesis, the phosphorylation of the 3'-hydroxyl group of ribose using ATP as a, phosphate donor. The protein from Haemophilus influenzae was cloned and, expressed, and its crystal structure was determined at 2.0-A resolution in, complex with ATP. The protein molecule consists of three domains: the, canonical nucleotide-binding domain with a five-stranded parallel, beta-sheet, the substrate-binding alpha-helical domain, and the lid domain, formed by a pair of alpha-helices. The overall topology of the protein, resembles the structures of nucleotide kinases. ATP binds in the P-loop in, a manner observed in other kinases. The CoA-binding site is located at the, interface of all three domains. The double-pocket structure of the, substrate-binding site is unusual for nucleotide kinases. Amino acid, residues implicated in substrate binding and catalysis have been, identified. The structure analysis suggests large domain movements during, the catalytic cycle.
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Dephospho-coenzyme A kinase catalyzes the final step in CoA biosynthesis, the phosphorylation of the 3'-hydroxyl group of ribose using ATP as a phosphate donor. The protein from Haemophilus influenzae was cloned and expressed, and its crystal structure was determined at 2.0-A resolution in complex with ATP. The protein molecule consists of three domains: the canonical nucleotide-binding domain with a five-stranded parallel beta-sheet, the substrate-binding alpha-helical domain, and the lid domain formed by a pair of alpha-helices. The overall topology of the protein resembles the structures of nucleotide kinases. ATP binds in the P-loop in a manner observed in other kinases. The CoA-binding site is located at the interface of all three domains. The double-pocket structure of the substrate-binding site is unusual for nucleotide kinases. Amino acid residues implicated in substrate binding and catalysis have been identified. The structure analysis suggests large domain movements during the catalytic cycle.
==About this Structure==
==About this Structure==
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1JJV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with SO4, HG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dephospho-CoA_kinase Dephospho-CoA kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.24 2.7.1.24] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JJV OCA].
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1JJV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HG:'>HG</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dephospho-CoA_kinase Dephospho-CoA kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.24 2.7.1.24] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JJV OCA].
==Reference==
==Reference==
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[[Category: Bonander, N.]]
[[Category: Bonander, N.]]
[[Category: Eisenstein, E.]]
[[Category: Eisenstein, E.]]
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[[Category: Gilliland, G.L.]]
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[[Category: Gilliland, G L.]]
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[[Category: Howard, A.J.]]
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[[Category: Howard, A J.]]
[[Category: Obmolova, G.]]
[[Category: Obmolova, G.]]
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[[Category: S2F, Structure.2.Function.Project.]]
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[[Category: S2F, Structure 2.Function Project.]]
[[Category: Teplyakov, A.]]
[[Category: Teplyakov, A.]]
[[Category: ATP]]
[[Category: ATP]]
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[[Category: structure 2 function project]]
[[Category: structure 2 function project]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:30 2008''

Revision as of 11:23, 21 February 2008


1jjv, resolution 2.Å

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DEPHOSPHO-COA KINASE IN COMPLEX WITH ATP

Overview

Dephospho-coenzyme A kinase catalyzes the final step in CoA biosynthesis, the phosphorylation of the 3'-hydroxyl group of ribose using ATP as a phosphate donor. The protein from Haemophilus influenzae was cloned and expressed, and its crystal structure was determined at 2.0-A resolution in complex with ATP. The protein molecule consists of three domains: the canonical nucleotide-binding domain with a five-stranded parallel beta-sheet, the substrate-binding alpha-helical domain, and the lid domain formed by a pair of alpha-helices. The overall topology of the protein resembles the structures of nucleotide kinases. ATP binds in the P-loop in a manner observed in other kinases. The CoA-binding site is located at the interface of all three domains. The double-pocket structure of the substrate-binding site is unusual for nucleotide kinases. Amino acid residues implicated in substrate binding and catalysis have been identified. The structure analysis suggests large domain movements during the catalytic cycle.

About this Structure

1JJV is a Single protein structure of sequence from Haemophilus influenzae with , and as ligands. Active as Dephospho-CoA kinase, with EC number 2.7.1.24 Full crystallographic information is available from OCA.

Reference

Crystal structure of dephospho-coenzyme A kinase from Haemophilus influenzae., Obmolova G, Teplyakov A, Bonander N, Eisenstein E, Howard AJ, Gilliland GL, J Struct Biol. 2001 Nov;136(2):119-25. PMID:11886213

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