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1xys

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(New page: 200px<br /><applet load="1xys" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xys, resolution 2.5&Aring;" /> '''CATALYTIC CORE OF XYL...)
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[[Image:1xys.jpg|left|200px]]<br /><applet load="1xys" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1xys, resolution 2.5&Aring;" />
 
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'''CATALYTIC CORE OF XYLANASE A E246C MUTANT'''<br />
 
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==Overview==
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==CATALYTIC CORE OF XYLANASE A E246C MUTANT==
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BACKGROUND: Sequence alignment suggests that xylanases evolved from two, ancestral proteins and therefore can be grouped into two families, designated F and G. Family F enzymes show no sequence similarity with any, known structure and their architecture is unknown. Studies of an inactive, enzyme-substrate complex will help to elucidate the structural basis of, binding and catalysis in the family F xylanases. RESULTS: We have, therefore determined the crystal structure of the catalytic domain of a, family F enzyme, Pseudomonas fluorescens subsp. cellulosa xylanase A, at, 2.5 A resolution and a crystallographic R-factor of 0.20. The structure, was solved using an engineered catalytic core in which the nucleophilic, glutamate was replaced by a cysteine. As expected, this yielded both, high-quality mercurial derivatives and an inactive enzyme which enabled, the preparation of the inactive enzyme-substrate complex in the crystal., We show that family F xylanases are eight-fold alpha/beta-barrels (TIM, barrels) with two active-site glutamates, one of which is the nucleophile, and the other the acid-base. Xylopentaose binds to five subsites A-E with, the cleaved bond between subsites D and E. Ca2+ binding, remote from the, active-site glutamates, stabilizes the structure and may be involved in, the binding of extended substrates. CONCLUSIONS: The architecture of P., fluorescens subsp. cellulosa has been determined crystallographically to, be a commonly occurring enzyme fold, the eight-fold alpha/beta-barrel., Xylopentaose binds across the carboxy-terminal end of the, alpha/beta-barrel in an active-site cleft which contains the two catalytic, glutamates.
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<StructureSection load='1xys' size='340' side='right'caption='[[1xys]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1xys]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellvibrio_japonicus Cellvibrio japonicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XYS FirstGlance]. <br>
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1XYS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cellvibrio_japonicus Cellvibrio japonicus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XYS OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xys OCA], [https://pdbe.org/1xys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xys RCSB], [https://www.ebi.ac.uk/pdbsum/1xys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xys ProSAT]</span></td></tr>
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Structure of the catalytic core of the family F xylanase from Pseudomonas fluorescens and identification of the xylopentaose-binding sites., Harris GW, Jenkins JA, Connerton I, Cummings N, Lo Leggio L, Scott M, Hazlewood GP, Laurie JI, Gilbert HJ, Pickersgill RW, Structure. 1994 Nov 15;2(11):1107-16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7881909 7881909]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/XYNA_CELJU XYNA_CELJU]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xy/1xys_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=1xys ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Cellvibrio japonicus]]
[[Category: Cellvibrio japonicus]]
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[[Category: Endo-1,4-beta-xylanase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Connerton I]]
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[[Category: Connerton, I.]]
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[[Category: Harris GW]]
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[[Category: Harris, G.W.]]
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[[Category: Jenkins JA]]
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[[Category: Jenkins, J.A.]]
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[[Category: Pickersgill RW]]
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[[Category: Pickersgill, R.W.]]
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[[Category: CA]]
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[[Category: family 10 of glycosyl-hydrolase]]
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[[Category: family f xylanase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:26:43 2007''
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CATALYTIC CORE OF XYLANASE A E246C MUTANT

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