1kgz

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(New page: 200px<br /><applet load="1kgz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kgz, resolution 2.4&Aring;" /> '''Crystal Structure Ana...)
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[[Image:1kgz.jpg|left|200px]]<br /><applet load="1kgz" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1kgz.jpg|left|200px]]<br /><applet load="1kgz" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1kgz, resolution 2.4&Aring;" />
caption="1kgz, resolution 2.4&Aring;" />
'''Crystal Structure Analysis of the Anthranilate Phosphoribosyltransferase from Erwinia carotovora (current name, Pectobacterium carotovorum)'''<br />
'''Crystal Structure Analysis of the Anthranilate Phosphoribosyltransferase from Erwinia carotovora (current name, Pectobacterium carotovorum)'''<br />
==Overview==
==Overview==
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The structure of anthranilate phosphoribosyltransferase from the, enterobacterium Pectobacterium carotovorum has been solved at 2.4 A in, complex with Mn(2+)-pyrophosphate, and at 1.9 A without ligands. The, enzyme structure has a novel phosphoribosyltransferase (PRT) fold and, displays close homology to the structures of pyrimidine nucleoside, phosphorylases. The enzyme is a homodimer with a monomer of 345 residues., Each monomer consists of two subdomains, alpha and alpha/beta, which form, a cleft containing the active site. The nature of the active site is, inferred from the trapped MnPPi complex and detailed knowledge of the, active sites of nucleoside phosphorylases. With the anthranilate (An)PRT, structure solved, the structures of all the enzymes required for, tryptophan biosynthesis are now known.
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The structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum has been solved at 2.4 A in complex with Mn(2+)-pyrophosphate, and at 1.9 A without ligands. The enzyme structure has a novel phosphoribosyltransferase (PRT) fold and displays close homology to the structures of pyrimidine nucleoside phosphorylases. The enzyme is a homodimer with a monomer of 345 residues. Each monomer consists of two subdomains, alpha and alpha/beta, which form a cleft containing the active site. The nature of the active site is inferred from the trapped MnPPi complex and detailed knowledge of the active sites of nucleoside phosphorylases. With the anthranilate (An)PRT structure solved, the structures of all the enzymes required for tryptophan biosynthesis are now known.
==About this Structure==
==About this Structure==
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1KGZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pectobacterium_carotovorum Pectobacterium carotovorum] with HG, MN and PRP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Anthranilate_phosphoribosyltransferase Anthranilate phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.18 2.4.2.18] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KGZ OCA].
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1KGZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pectobacterium_carotovorum Pectobacterium carotovorum] with <scene name='pdbligand=HG:'>HG</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=PRP:'>PRP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Anthranilate_phosphoribosyltransferase Anthranilate phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.18 2.4.2.18] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KGZ OCA].
==Reference==
==Reference==
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[[Category: Kim, C.]]
[[Category: Kim, C.]]
[[Category: Madhusudan]]
[[Category: Madhusudan]]
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[[Category: Mills, S.E.]]
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[[Category: Mills, S E.]]
[[Category: Spraggon, G.]]
[[Category: Spraggon, G.]]
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[[Category: Xuong, N.H.]]
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[[Category: Xuong, N H.]]
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[[Category: Yee, M.C.]]
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[[Category: Yee, M C.]]
[[Category: HG]]
[[Category: HG]]
[[Category: MN]]
[[Category: MN]]
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[[Category: type 3 prt fold]]
[[Category: type 3 prt fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:20:54 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:34:06 2008''

Revision as of 11:34, 21 February 2008


1kgz, resolution 2.4Å

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Crystal Structure Analysis of the Anthranilate Phosphoribosyltransferase from Erwinia carotovora (current name, Pectobacterium carotovorum)

Overview

The structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum has been solved at 2.4 A in complex with Mn(2+)-pyrophosphate, and at 1.9 A without ligands. The enzyme structure has a novel phosphoribosyltransferase (PRT) fold and displays close homology to the structures of pyrimidine nucleoside phosphorylases. The enzyme is a homodimer with a monomer of 345 residues. Each monomer consists of two subdomains, alpha and alpha/beta, which form a cleft containing the active site. The nature of the active site is inferred from the trapped MnPPi complex and detailed knowledge of the active sites of nucleoside phosphorylases. With the anthranilate (An)PRT structure solved, the structures of all the enzymes required for tryptophan biosynthesis are now known.

About this Structure

1KGZ is a Single protein structure of sequence from Pectobacterium carotovorum with , and as ligands. Active as Anthranilate phosphoribosyltransferase, with EC number 2.4.2.18 Full crystallographic information is available from OCA.

Reference

The crystal structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum., Kim C, Xuong NH, Edwards S, Madhusudan, Yee MC, Spraggon G, Mills SE, FEBS Lett. 2002 Jul 17;523(1-3):239-46. PMID:12123839

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