1sqj
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Oligoxyloglucan_reducing-end-specific_cellobiohydrolase Oligoxyloglucan reducing-end-specific cellobiohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.150 3.2.1.150] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Oligoxyloglucan_reducing-end-specific_cellobiohydrolase Oligoxyloglucan reducing-end-specific cellobiohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.150 3.2.1.150] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sqj OCA], [http://www.ebi.ac.uk/pdbsum/1sqj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sqj RCSB]</span> | ||
}} | }} | ||
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[[Category: beta-propeller]] | [[Category: beta-propeller]] | ||
| - | ''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 23:45:38 2008'' |
Revision as of 20:45, 30 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Oligoxyloglucan reducing-end-specific cellobiohydrolase, with EC number 3.2.1.150 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Analysis of Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH)
Overview
Oligoxyloglucan reducing-end-specific cellobiohydrolase (OXG-RCBH; EC 3.2.1.150) is an exoglucanase that recognizes the reducing end of oligoxyloglucan and releases two glucosyl residue segments from the main chain. The X-ray crystal structure of OXG-RCBH determined at 2.2 A resolution reveals a unique feature of this enzyme; OXG-RCBH consists of a tandem repeat of two similar domains, which are both folded into seven-bladed beta-propeller structures. The sequence alignment of the propeller blades, based on the structure, indicates that a weak repeat of the amino acid sequence occurred seven times to construct each domain. There is a cleft that can accommodate the substrate oligosaccharide between the two domains, which is a putative substrate binding subsite. Mutation of either Asp35 or Asp465, located in the putative catalytic center, to Asn resulted in a protein with no detectable catalytic activity, indicating the critical role of these amino acids in catalysis.
About this Structure
1SQJ is a Single protein structure of sequence from Geotrichum sp. m128. Full crystallographic information is available from OCA.
Reference
Tandem repeat of a seven-bladed beta-propeller domain in oligoxyloglucan reducing-end-specific cellobiohydrolase., Yaoi K, Kondo H, Noro N, Suzuki M, Tsuda S, Mitsuishi Y, Structure. 2004 Jul;12(7):1209-17. PMID:15242597
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