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| [[Image:1nof.gif|left|200px]]<br /><applet load="1nof" size="350" color="white" frame="true" align="right" spinBox="true"
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| caption="1nof, resolution 1.42Å" />
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| '''THE FIRST CRYSTALLOGRAPHIC STRUCTURE OF A XYLANASE FROM GLYCOSYL HYDROLASE FAMILY 5: IMPLICATIONS FOR CATALYSIS'''<br />
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| ==Overview== | | ==THE FIRST CRYSTALLOGRAPHIC STRUCTURE OF A XYLANASE FROM GLYCOSYL HYDROLASE FAMILY 5: IMPLICATIONS FOR CATALYSIS== |
| The room-temperature structure of xylanase (EC 3.2.1.8) from the bacterial plant pathogen Erwinia chrysanthemi expressed in Escherichia coli, a 45 kDa, 413-amino acid protein belonging to glycoside hydrolase family 5, has been determined by multiple isomorphous replacement and refined to a resolution of 1.42 A. This represents the first structure of a xylanase not belonging to either glycoside hydrolase family 10 or family 11. The enzyme is composed of two domains similar to most family 10 xylanases and the alpha-amylases. The catalytic domain (residues 46-315) has a (beta/alpha)(8)-barrel motif with a binding cleft along the C-terminal side of the beta-barrel. The catalytic residues, Glu165 and Glu253, determined by correspondence to other family 5 and family 10 glycoside hydrolases, lie inside this cleft on the C-terminal ends of beta-strands 4 and 7, respectively, with an O(epsilon)2...O(epsilon)1 distance of 4.22 A. The smaller domain (residues 31-43 and 323-413) has a beta(9)-barrel motif with five of the strands interfacing with alpha-helices 7 and 8 of the catalytic domain. The first 13 N-terminal residues form one beta-strand of this domain. Residues 44, 45, and 316-322 form the linkers between this domain and the catalytic domain.
| | <StructureSection load='1nof' size='340' side='right'caption='[[1nof]], [[Resolution|resolution]] 1.42Å' scene=''> |
| | | == Structural highlights == |
| ==About this Structure== | | <table><tr><td colspan='2'>[[1nof]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dickeya_chrysanthemi Dickeya chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NOF FirstGlance]. <br> |
| 1NOF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi] with <scene name='pdbligand=ACT:'>ACT</scene> 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] Known structural/functional Sites: <scene name='pdbsite=ACI:Catalytic+Acid/Base'>ACI</scene> and <scene name='pdbsite=NUC:Catalytic+Nucleophile'>NUC</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NOF OCA].
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.42Å</td></tr> |
| | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> |
| ==Reference==
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nof OCA], [https://pdbe.org/1nof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nof RCSB], [https://www.ebi.ac.uk/pdbsum/1nof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nof ProSAT]</span></td></tr> |
| First crystallographic structure of a xylanase from glycoside hydrolase family 5: implications for catalysis., Larson SB, Day J, Barba de la Rosa AP, Keen NT, McPherson A, Biochemistry. 2003 Jul 22;42(28):8411-22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12859186 12859186]
| | </table> |
| [[Category: Endo-1,4-beta-xylanase]] | | == Function == |
| [[Category: Erwinia chrysanthemi]] | | [https://www.uniprot.org/uniprot/Q46961_DICCH Q46961_DICCH] |
| [[Category: Single protein]] | | == Evolutionary Conservation == |
| [[Category: Day, J.]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| [[Category: Keen, N T.]] | | Check<jmol> |
| [[Category: Larson, S B.]] | | <jmolCheckbox> |
| [[Category: McPherson, A.]] | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/no/1nof_consurf.spt"</scriptWhenChecked> |
| [[Category: Rosa, A P.Barba De La.]] | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| [[Category: ACT]] | | <text>to colour the structure by Evolutionary Conservation</text> |
| [[Category: carbohydrate-binding module]] | | </jmolCheckbox> |
| [[Category: catalytic domain]] | | </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=1nof ConSurf]. |
| [[Category: glycohydrolase family 5]] | | <div style="clear:both"></div> |
| [[Category: xylanase]]
| | __TOC__ |
| | | </StructureSection> |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:16 2008''
| | [[Category: Dickeya chrysanthemi]] |
| | [[Category: Large Structures]] |
| | [[Category: Barba De La Rosa AP]] |
| | [[Category: Day J]] |
| | [[Category: Keen NT]] |
| | [[Category: Larson SB]] |
| | [[Category: McPherson A]] |