1clx: Difference between revisions
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|PDB= 1clx |SIZE=350|CAPTION= <scene name='initialview01'>1clx</scene>, resolution 1.8Å | |PDB= 1clx |SIZE=350|CAPTION= <scene name='initialview01'>1clx</scene>, resolution 1.8Å | ||
|SITE= <scene name='pdbsite=CAT:Two+Catalytic+Residues+Acid-Base+GLU+127+Nucleophile+GLU+246'>CAT</scene> | |SITE= <scene name='pdbsite=CAT:Two+Catalytic+Residues+Acid-Base+GLU+127+Nucleophile+GLU+246'>CAT</scene> | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= TRUNCATED XYNA (CODONS 264-611 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155077 Cellvibrio japonicus]) | |GENE= TRUNCATED XYNA (CODONS 264-611 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155077 Cellvibrio japonicus]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1clx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1clx OCA], [http://www.ebi.ac.uk/pdbsum/1clx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1clx RCSB]</span> | |||
}} | }} | ||
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[[Category: Jenkins, J A.]] | [[Category: Jenkins, J A.]] | ||
[[Category: Pickersgill, R W.]] | [[Category: Pickersgill, R W.]] | ||
[[Category: family-f xylanase family 10 glycosyl-hydrolase]] | [[Category: family-f xylanase family 10 glycosyl-hydrolase]] | ||
[[Category: xylanase]] | [[Category: xylanase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:24:09 2008'' | ||
Revision as of 19:24, 30 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Gene: | TRUNCATED XYNA (CODONS 264-611 (Cellvibrio japonicus) | ||||||
| Activity: | Endo-1,4-beta-xylanase, with EC number 3.2.1.8 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CATALYTIC CORE OF XYLANASE A
OverviewOverview
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 StructureAbout this Structure
1CLX is a Single protein structure of sequence from Cellvibrio japonicus. Full crystallographic information is available from OCA.
ReferenceReference
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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