1vht

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[[Image:1vht.gif|left|200px]]<br /><applet load="1vht" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1vht.gif|left|200px]]
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caption="1vht, resolution 1.59&Aring;" />
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'''Crystal structure of dephospho-coA kinase with bis(adenosine)-5'-triphosphate'''<br />
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{{Structure
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|PDB= 1vht |SIZE=350|CAPTION= <scene name='initialview01'>1vht</scene>, resolution 1.59&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=BA3:BIS(ADENOSINE)-5'-TRIPHOSPHATE'>BA3</scene>
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|ACTIVITY= [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]
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|GENE= COAE, B0103, Z0113, ECS0107 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''Crystal structure of dephospho-coA kinase with bis(adenosine)-5'-triphosphate'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1VHT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=BA3:'>BA3</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=1VHT OCA].
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1VHT 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=1VHT OCA].
==Reference==
==Reference==
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Structural analysis of a set of proteins resulting from a bacterial genomics project., Badger J, Sauder JM, Adams JM, Antonysamy S, Bain K, Bergseid MG, Buchanan SG, Buchanan MD, Batiyenko Y, Christopher JA, Emtage S, Eroshkina A, Feil I, Furlong EB, Gajiwala KS, Gao X, He D, Hendle J, Huber A, Hoda K, Kearins P, Kissinger C, Laubert B, Lewis HA, Lin J, Loomis K, Lorimer D, Louie G, Maletic M, Marsh CD, Miller I, Molinari J, Muller-Dieckmann HJ, Newman JM, Noland BW, Pagarigan B, Park F, Peat TS, Post KW, Radojicic S, Ramos A, Romero R, Rutter ME, Sanderson WE, Schwinn KD, Tresser J, Winhoven J, Wright TA, Wu L, Xu J, Harris TJ, Proteins. 2005 Sep 1;60(4):787-96. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16021622 16021622]
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Structural analysis of a set of proteins resulting from a bacterial genomics project., Badger J, Sauder JM, Adams JM, Antonysamy S, Bain K, Bergseid MG, Buchanan SG, Buchanan MD, Batiyenko Y, Christopher JA, Emtage S, Eroshkina A, Feil I, Furlong EB, Gajiwala KS, Gao X, He D, Hendle J, Huber A, Hoda K, Kearins P, Kissinger C, Laubert B, Lewis HA, Lin J, Loomis K, Lorimer D, Louie G, Maletic M, Marsh CD, Miller I, Molinari J, Muller-Dieckmann HJ, Newman JM, Noland BW, Pagarigan B, Park F, Peat TS, Post KW, Radojicic S, Ramos A, Romero R, Rutter ME, Sanderson WE, Schwinn KD, Tresser J, Winhoven J, Wright TA, Wu L, Xu J, Harris TJ, Proteins. 2005 Sep 1;60(4):787-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16021622 16021622]
[[Category: Dephospho-CoA kinase]]
[[Category: Dephospho-CoA kinase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: ACT]]
[[Category: ACT]]
[[Category: BA3]]
[[Category: BA3]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:35:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:45:47 2008''

Revision as of 12:45, 20 March 2008


PDB ID 1vht

Drag the structure with the mouse to rotate
, resolution 1.59Å
Ligands: and
Gene: COAE, B0103, Z0113, ECS0107 (Escherichia coli)
Activity: Dephospho-CoA kinase, with EC number 2.7.1.24
Coordinates: save as pdb, mmCIF, xml



Crystal structure of dephospho-coA kinase with bis(adenosine)-5'-triphosphate


Overview

The targets of the Structural GenomiX (SGX) bacterial genomics project were proteins conserved in multiple prokaryotic organisms with no obvious sequence homolog in the Protein Data Bank of known structures. The outcome of this work was 80 structures, covering 60 unique sequences and 49 different genes. Experimental phase determination from proteins incorporating Se-Met was carried out for 45 structures with most of the remainder solved by molecular replacement using members of the experimentally phased set as search models. An automated tool was developed to deposit these structures in the Protein Data Bank, along with the associated X-ray diffraction data (including refined experimental phases) and experimentally confirmed sequences. BLAST comparisons of the SGX structures with structures that had appeared in the Protein Data Bank over the intervening 3.5 years since the SGX target list had been compiled identified homologs for 49 of the 60 unique sequences represented by the SGX structures. This result indicates that, for bacterial structures that are relatively easy to express, purify, and crystallize, the structural coverage of gene space is proceeding rapidly. More distant sequence-structure relationships between the SGX and PDB structures were investigated using PDB-BLAST and Combinatorial Extension (CE). Only one structure, SufD, has a truly unique topology compared to all folds in the PDB.

About this Structure

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

Reference

Structural analysis of a set of proteins resulting from a bacterial genomics project., Badger J, Sauder JM, Adams JM, Antonysamy S, Bain K, Bergseid MG, Buchanan SG, Buchanan MD, Batiyenko Y, Christopher JA, Emtage S, Eroshkina A, Feil I, Furlong EB, Gajiwala KS, Gao X, He D, Hendle J, Huber A, Hoda K, Kearins P, Kissinger C, Laubert B, Lewis HA, Lin J, Loomis K, Lorimer D, Louie G, Maletic M, Marsh CD, Miller I, Molinari J, Muller-Dieckmann HJ, Newman JM, Noland BW, Pagarigan B, Park F, Peat TS, Post KW, Radojicic S, Ramos A, Romero R, Rutter ME, Sanderson WE, Schwinn KD, Tresser J, Winhoven J, Wright TA, Wu L, Xu J, Harris TJ, Proteins. 2005 Sep 1;60(4):787-96. PMID:16021622

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