1GOO
Thermostable xylanase I from Thermoascus aurantiacus - Cryocooled glycerol complex
Summary for 1GOO
| Entry DOI | 10.2210/pdb1goo/pdb |
| Descriptor | ENDO-1,4-BETA-XYLANASE, GLYCEROL (3 entities in total) |
| Functional Keywords | family 10, plant cell wall degradation, hydrolase |
| Biological source | THERMOASCUS AURANTIACUS |
| Total number of polymer chains | 1 |
| Total formula weight | 32982.81 |
| Authors | Eckert, K.,Andrei, C.,Larsen, S.,Lo Leggio, L. (deposition date: 2001-10-22, release date: 2001-12-03, Last modification date: 2024-10-23) |
| Primary citation | Lo Leggio, L.,Kalogiannis, S.,Eckert, K.,Teixeira, S.C.M.,Bhat, M.K.,Andrei, C.,Pickersgill, R.W.,Larsen, S. Substrate Specificity and Subsite Mobility in T. Aurantiacus Xylanase 10A FEBS Lett., 509:303-, 2001 Cited by PubMed Abstract: 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. PubMed: 11741607DOI: 10.1016/S0014-5793(01)03177-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.87 Å) |
Structure validation
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