1xib
From Proteopedia
(New page: 200px<br /><applet load="1xib" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xib, resolution 1.6Å" /> '''MODES OF BINDING SUBS...) |
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| - | [[Image:1xib.jpg|left|200px]]<br /><applet load="1xib" size=" | + | [[Image:1xib.jpg|left|200px]]<br /><applet load="1xib" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xib, resolution 1.6Å" /> | caption="1xib, resolution 1.6Å" /> | ||
'''MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE'''<br /> | '''MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Studies of binding of substrates and inhibitors of the enzyme D-xylose | + | Studies of binding of substrates and inhibitors of the enzyme D-xylose isomerase show, from X-ray diffraction data at 1.6-1.9 A resolution, that there are a variety of binding modes. These vary in the manner in which the substrate or its analogue extend, on binding, across the carboxy end of the (betaalpha)(8)-barrel structure. These binding sites are His54 and the metal ion (magnesium or manganese) that is held in place by Glul81, Asp245, Glu217 and Asp287. Possible catalytic groups have been identified in proposed mechanisms and their role in the binding of ligands is illustrated. |
==About this Structure== | ==About this Structure== | ||
| - | 1XIB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_rubiginosus Streptomyces rubiginosus] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 1XIB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_rubiginosus Streptomyces rubiginosus] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entries 7XIA and 2XIA. Active as [http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XIB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Streptomyces rubiginosus]] | [[Category: Streptomyces rubiginosus]] | ||
[[Category: Xylose isomerase]] | [[Category: Xylose isomerase]] | ||
| - | [[Category: Carrell, H | + | [[Category: Carrell, H L.]] |
| - | [[Category: Glusker, J | + | [[Category: Glusker, J P.]] |
[[Category: MN]] | [[Category: MN]] | ||
[[Category: isomerase(intramolecular oxidoreductse)]] | [[Category: isomerase(intramolecular oxidoreductse)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:55:12 2008'' |
Revision as of 13:55, 21 February 2008
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MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE
Overview
Studies of binding of substrates and inhibitors of the enzyme D-xylose isomerase show, from X-ray diffraction data at 1.6-1.9 A resolution, that there are a variety of binding modes. These vary in the manner in which the substrate or its analogue extend, on binding, across the carboxy end of the (betaalpha)(8)-barrel structure. These binding sites are His54 and the metal ion (magnesium or manganese) that is held in place by Glul81, Asp245, Glu217 and Asp287. Possible catalytic groups have been identified in proposed mechanisms and their role in the binding of ligands is illustrated.
About this Structure
1XIB is a Single protein structure of sequence from Streptomyces rubiginosus with as ligand. This structure supersedes the now removed PDB entries 7XIA and 2XIA. Active as Xylose isomerase, with EC number 5.3.1.5 Full crystallographic information is available from OCA.
Reference
Modes of binding substrates and their analogues to the enzyme D-xylose isomerase., Carrell HL, Hoier H, Glusker JP, Acta Crystallogr D Biol Crystallogr. 1994 Mar 1;50(Pt 2):113-23. PMID:15299449
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