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| | <StructureSection load='1gok' size='340' side='right'caption='[[1gok]], [[Resolution|resolution]] 1.14Å' scene=''> | | <StructureSection load='1gok' size='340' side='right'caption='[[1gok]], [[Resolution|resolution]] 1.14Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gok]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoascus_aurantiacus Thermoascus aurantiacus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1tax 1tax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GOK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GOK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gok]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoascus_aurantiacus Thermoascus aurantiacus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1tax 1tax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GOK FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.14Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fxm|1fxm]], [[1tax|1tax]], [[1tix|1tix]], [[1gom|1gom]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gok OCA], [https://pdbe.org/1gok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gok RCSB], [https://www.ebi.ac.uk/pdbsum/1gok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gok ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gok OCA], [http://pdbe.org/1gok PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gok RCSB], [http://www.ebi.ac.uk/pdbsum/1gok PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gok ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/XYNA_THEAU XYNA_THEAU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Endo-1,4-beta-xylanase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Thermoascus aurantiacus]] | | [[Category: Thermoascus aurantiacus]] |
| - | [[Category: Leggio, L Lo]] | + | [[Category: Lo Leggio L]] |
| - | [[Category: Pickersgill, R W]] | + | [[Category: Pickersgill RW]] |
| - | [[Category: Family 10]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Plant cell wall degradation]]
| + | |
| - | [[Category: Xylanase]]
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| Structural highlights
Function
XYNA_THEAU
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lo Leggio L, Kalogiannis S, Eckert K, Teixeira SC, Bhat MK, Andrei C, Pickersgill RW, Larsen S. Substrate specificity and subsite mobility in T. aurantiacus xylanase 10A. FEBS Lett. 2001 Dec 7;509(2):303-8. PMID:11741607
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