1gom
From Proteopedia
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|PDB= 1gom |SIZE=350|CAPTION= <scene name='initialview01'>1gom</scene>, resolution 1.92Å | |PDB= 1gom |SIZE=350|CAPTION= <scene name='initialview01'>1gom</scene>, resolution 1.92Å | ||
|SITE= <scene name='pdbsite=ACI:Catalytic+Nucleophile'>ACI</scene> | |SITE= <scene name='pdbsite=ACI:Catalytic+Nucleophile'>ACI</scene> | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gom FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gom OCA], [http://www.ebi.ac.uk/pdbsum/1gom PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gom RCSB]</span> | ||
}} | }} | ||
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[[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 20:48:18 2008'' |
Revision as of 17:48, 30 March 2008
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| , resolution 1.92Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Endo-1,4-beta-xylanase, with EC number 3.2.1.8 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THERMOSTABLE XYLANASE I FROM THERMOASCUS AURANTIACUS-CRYSTAL FORM I
Overview
The substrate specificity of Thermoascus aurantiacus xylanase 10A (TAX) has been investigated both biochemically and structurally. High resolution crystallographic analyses at 291 K and 100 K of TAX complexes with xylobiose show that the ligand is in its alpha anomeric conformation and provide a rationale for specificity on p-nitrophenyl glycosides at the -1 and -2 subsites. Trp 275, which is disordered in uncomplexed structures, is stabilised by its interaction with xylobiose. Two structural subsets in family 10 are identified, which differ by the presence or absence of a short helical stretch in the eighth betaalpha-loop of the TIM barrel, the loop bearing Trp 275. This structural difference is discussed in the context of Trp 275 mobility and xylanase function.
About this Structure
1GOM is a Single protein structure of sequence from Thermoascus aurantiacus. This structure supersedes the now removed PDB entry 1TIX. Full crystallographic information is available from OCA.
Reference
Substrate specificity and subsite mobility in T. aurantiacus xylanase 10A., Lo Leggio L, Kalogiannis S, Eckert K, Teixeira SC, Bhat MK, Andrei C, Pickersgill RW, Larsen S, FEBS Lett. 2001 Dec 7;509(2):303-8. PMID:11741607
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