1xas: Difference between revisions
No edit summary |
No edit summary |
||
Line 5: | Line 5: | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
|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= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xas OCA], [http://www.ebi.ac.uk/pdbsum/1xas PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xas RCSB]</span> | |||
}} | }} | ||
Line 27: | Line 30: | ||
[[Category: xylanase some]] | [[Category: xylanase some]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:47:03 2008'' |
Revision as of 00:47, 31 March 2008
| |||||||
, resolution 2.6Å | |||||||
---|---|---|---|---|---|---|---|
Activity: | Endo-1,4-beta-xylanase, with EC number 3.2.1.8 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CRYSTAL STRUCTURE, AT 2.6 ANGSTROMS RESOLUTION, OF THE STREPTOMYCES LIVIDANS XYLANASE A, A MEMBER OF THE F FAMILY OF BETA-1,4-D-GLYCANSES
OverviewOverview
The crystal structure of the 32-kDa catalytic domain of the Streptomyces lividans xylanase A was solved by molecular isomorphous replacement methods and subsequently refined at 2.6-A resolution to a conventional crystallographic R factor of 0.21. This is the first successful structure determination of a member of the F family of endo-beta-1,4-D-glycanases. Unlike the recently determined xylanases of the G family (Wakarchuk, W. W., Campbell, R. L., Sung, W. L., Davoodi, J., and Yaguchi, M. (1994) Protein Sci. 3, 467-475), where the catalytic domains have a unique beta-sheet structure, the 32-kDa domain of the S. lividans xylanase A is folded into a complete (alpha/beta)8 barrel, the first such fold observed among beta-1,4-D-glycanases. The active site is located at the carbonyl end of the beta barrel. The crystal structure supports the earlier assignment of Glu-128 and Glu-236 as the catalytic amino acids (Moreau, A., Roberge, M., Manin, C., Shareck, F., Kluepfel, D., and Morosoli, R. (1994) Biochem. J., in press).
About this StructureAbout this Structure
1XAS is a Single protein structure of sequence from Streptomyces lividans. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure, at 2.6-A resolution, of the Streptomyces lividans xylanase A, a member of the F family of beta-1,4-D-glycanases., Derewenda U, Swenson L, Green R, Wei Y, Morosoli R, Shareck F, Kluepfel D, Derewenda ZS, J Biol Chem. 1994 Aug 19;269(33):20811-4. PMID:8063693
Page seeded by OCA on Mon Mar 31 00:47:03 2008