1clx
From Proteopedia
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| - | [[Image:1clx.gif|left|200px]]<br /><applet load="1clx" size=" | + | [[Image:1clx.gif|left|200px]]<br /><applet load="1clx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1clx, resolution 1.8Å" /> | caption="1clx, resolution 1.8Å" /> | ||
'''CATALYTIC CORE OF XYLANASE A'''<br /> | '''CATALYTIC CORE OF XYLANASE A'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CLX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cellvibrio_japonicus Cellvibrio japonicus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] Known structural/functional Site: <scene name='pdbsite=CAT:Two Catalytic Residues Acid-Base GLU 127 Nucleophile GLU 246'>CAT</scene>. Full crystallographic information is available from [http:// | + | 1CLX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cellvibrio_japonicus Cellvibrio japonicus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] Known structural/functional Site: <scene name='pdbsite=CAT:Two+Catalytic+Residues+Acid-Base+GLU+127+Nucleophile+GLU+246'>CAT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CLX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: xylanase]] | [[Category: xylanase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:34:45 2008'' |
Revision as of 07:34, 3 February 2008
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CATALYTIC CORE OF XYLANASE A
Overview
The three-dimensional structure of native xylanase A from Pseudomonas, flouorescens subspecies cellulosa has been refined at 1.8 A resolution., The space group is P2(1)2(1)2(1) with four molecules in the asymmetric, unit. The final model has an R factor of 0.166 for 103 749 reflections, with the four molecules refined independently. The tertiary structure, consists of an eightfold beta/alpha-barrel, the so-called TIM-barrel fold., The active site is in an open cleft at the carboxy-terminal end of the, beta/alpha-barrel, and the active-site residues are a pair of glutamates, Glu127 on strand 4 and Glu246 on strand 7. Both these catalytic glutamate, residues are found on beta-bulges. An atypically long loop after strand 7, is stabilized by calcium. Unusual features include a non-proline, cis-peptide residue Ala80 which is found on a beta-bulge at the end of, beta-strand 3. The three beta-bulge type distortions occurring on, beta-strands 3, 4 and 7 are functionally significant as they serve to, orient important active-site residues. The active-site residues are, further held in place by an extensive hydrogen-bonding network of, active-site residues in the catalytic site of xylanase A. A chain of well, ordered water molecules occupies the substrate-binding cleft, some or all, of which are expelled on binding of the substrate.
About this Structure
1CLX is a Single protein structure of sequence from Cellvibrio japonicus with as ligand. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Refined crystal structure of the catalytic domain of xylanase A from Pseudomonas fluorescens at 1.8 A resolution., Harris GW, Jenkins JA, Connerton I, Pickersgill RW, Acta Crystallogr D Biol Crystallogr. 1996 Mar 1;52(Pt 2):393-401. PMID:15299710
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