1k6a

<StructureSection load='1k6a' size='340' side='right' caption='[[1k6a]], [[Resolution|resolution]] 1.14&Aring;' scene=''>

<table><tr><td colspan='2'>[[1k6a]] 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=1fxm 1fxm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K6A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K6A FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fxm|1fxm]], [[1tax|1tax]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k6a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1k6a RCSB], [http://www.ebi.ac.uk/pdbsum/1k6a PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k6/1k6a_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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== 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<ref>PMID:11741607</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Endo-1,4-beta-xylanase]]

[[Category: Andrei, C]]

[[Category: Bhat, M K]]

[[Category: Eckert, K]]

[[Category: Kalogiannis, S]]

[[Category: Larsen, S]]

[[Category: Leggio, L Lo]]

[[Category: Pickersgill, R W]]

[[Category: Teixeira, S C.M]]

[[Category: Hydrolase]]