2vep
From Proteopedia
(New page: 200px<br /><applet load="2vep" size="350" color="white" frame="true" align="right" spinBox="true" caption="2vep, resolution 1.80Å" /> '''CRYSTAL STRUCTURE OF...) |
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==Overview== | ==Overview== | ||
| - | Two structures of phosphoribosyl isomerase A (PriA) from Streptomyces | + | Two structures of phosphoribosyl isomerase A (PriA) from Streptomyces coelicolor, involved in both histidine and tryptophan biosynthesis, were solved at 1.8A resolution. A closed conformer was obtained, which represents the first complete structure of PriA, revealing hitherto unnoticed molecular interactions and the occurrence of conformational changes. Inspection of these conformers, including ligand-docking simulations, allowed identification of residues involved in substrate recognition, chemical catalysis and conformational changes. These predictions were validated by mutagenesis and functional analysis. Arg19 and Ser81 were shown to play critical roles within the carboxyl and amino phosphate-binding sites, respectively; the catalytic residues Asp11 and Asp130 are responsible for both activities; and Thr166 and Asp171, which make an unusual contact, are likely to elicit the conformational changes needed for adopting the active site architectures. This represents the first report of the structure/function relationship of this (betaalpha)8-isomerase. |
==About this Structure== | ==About this Structure== | ||
| - | 2VEP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=AC1:So4 Binding Site For Chain A'>AC1</scene> and <scene name='pdbsite=AC2:So4 Binding Site For Chain A'>AC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VEP OCA]. | + | 2VEP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene> and <scene name='pdbsite=AC2:So4+Binding+Site+For+Chain+A'>AC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VEP OCA]. |
==Reference== | ==Reference== | ||
| - | The structure/function relationship of a dual-substrate (betaalpha) | + | The structure/function relationship of a dual-substrate (betaalpha)8-isomerase., Wright H, Noda-Garcia L, Ochoa-Leyva A, Hodgson DA, Fulop V, Barona-Gomez F, Biochem Biophys Res Commun. 2008 Jan 4;365(1):16-21. Epub 2007 Oct 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17967415 17967415] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces coelicolor]] | [[Category: Streptomyces coelicolor]] | ||
[[Category: Barona-Gomez, F.]] | [[Category: Barona-Gomez, F.]] | ||
[[Category: Fulop, V.]] | [[Category: Fulop, V.]] | ||
| - | [[Category: Hodgson, D | + | [[Category: Hodgson, D A.]] |
[[Category: Noda-Garcia, L.]] | [[Category: Noda-Garcia, L.]] | ||
[[Category: Ochoa-Leyva, A.]] | [[Category: Ochoa-Leyva, A.]] | ||
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[[Category: tryptophan biosynthesis]] | [[Category: tryptophan biosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:55:17 2008'' |
Revision as of 16:55, 21 February 2008
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CRYSTAL STRUCTURE OF THE FULL LENGTH BIFUNCTIONAL ENZYME PRIA
Overview
Two structures of phosphoribosyl isomerase A (PriA) from Streptomyces coelicolor, involved in both histidine and tryptophan biosynthesis, were solved at 1.8A resolution. A closed conformer was obtained, which represents the first complete structure of PriA, revealing hitherto unnoticed molecular interactions and the occurrence of conformational changes. Inspection of these conformers, including ligand-docking simulations, allowed identification of residues involved in substrate recognition, chemical catalysis and conformational changes. These predictions were validated by mutagenesis and functional analysis. Arg19 and Ser81 were shown to play critical roles within the carboxyl and amino phosphate-binding sites, respectively; the catalytic residues Asp11 and Asp130 are responsible for both activities; and Thr166 and Asp171, which make an unusual contact, are likely to elicit the conformational changes needed for adopting the active site architectures. This represents the first report of the structure/function relationship of this (betaalpha)8-isomerase.
About this Structure
2VEP is a Single protein structure of sequence from Streptomyces coelicolor with as ligand. Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
The structure/function relationship of a dual-substrate (betaalpha)8-isomerase., Wright H, Noda-Garcia L, Ochoa-Leyva A, Hodgson DA, Fulop V, Barona-Gomez F, Biochem Biophys Res Commun. 2008 Jan 4;365(1):16-21. Epub 2007 Oct 29. PMID:17967415
Page seeded by OCA on Thu Feb 21 18:55:17 2008
Categories: Single protein | Streptomyces coelicolor | Barona-Gomez, F. | Fulop, V. | Hodgson, D A. | Noda-Garcia, L. | Ochoa-Leyva, A. | Wright, H. | SO4 | (beta-alpha)8-barrel | Amino-acid biosynthesis | Aromatic amino acid biosynthesis | Cytoplasm | Evolution of substrate specificity | Histidine biosynthesis | Isomerase | Pria | Tryptophan biosynthesis
