1m4w

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{{Seed}}
 
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[[Image:1m4w.png|left|200px]]
 
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==Thermophilic b-1,4-xylanase from Nonomuraea flexuosa==
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The line below this paragraph, containing "STRUCTURE_1m4w", creates the "Structure Box" on the page.
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<StructureSection load='1m4w' size='340' side='right'caption='[[1m4w]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1m4w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermopolyspora_flexuosa Thermopolyspora flexuosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M4W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M4W FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.1&#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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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{{STRUCTURE_1m4w| PDB=1m4w | SCENE= }}
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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=1m4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m4w OCA], [https://pdbe.org/1m4w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m4w RCSB], [https://www.ebi.ac.uk/pdbsum/1m4w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m4w ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8GMV7_9ACTN Q8GMV7_9ACTN]
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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/m4/1m4w_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1m4w ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structures of thermophilic xylanases from Chaetomium thermophilum and Nonomuraea flexuosa were determined at 1.75 and 2.1 A resolution, respectively. Both enzymes have the overall fold typical to family 11 xylanases with two highly twisted beta-sheets forming a large cleft. The comparison of 12 crystal structures of family 11 xylanases from both mesophilic and thermophilic organisms showed that the structures of different xylanases are very similar. The sequence identity differences correlated well with the structural differences. Several minor modifications appeared to be responsible for the increased thermal stability of family 11 xylanases: (a) higher Thr : Ser ratio (b) increased number of charged residues, especially Arg, resulting in enhanced polar interactions, and (c) improved stabilization of secondary structures involved the higher number of residues in the beta-strands and stabilization of the alpha-helix region. Some members of family 11 xylanases have a unique strategy to improve their stability, such as a higher number of ion pairs or aromatic residues on protein surface, a more compact structure, a tighter packing, and insertions at some regions resulting in enhanced interactions.
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===Thermophilic b-1,4-xylanase from Nonomuraea flexuosa===
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Three-dimensional structures of thermophilic beta-1,4-xylanases from Chaetomium thermophilum and Nonomuraea flexuosa. Comparison of twelve xylanases in relation to their thermal stability.,Hakulinen N, Turunen O, Janis J, Leisola M, Rouvinen J Eur J Biochem. 2003 Apr;270(7):1399-412. PMID:12653995<ref>PMID:12653995</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_12653995}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1m4w" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12653995 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12653995}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1M4W is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Thermopolyspora_flexuosa Thermopolyspora flexuosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M4W OCA].
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==Reference==
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<ref group="xtra">PMID:12653995</ref><references group="xtra"/>
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[[Category: Endo-1,4-beta-xylanase]]
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[[Category: Thermopolyspora flexuosa]]
[[Category: Thermopolyspora flexuosa]]
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[[Category: Hakulinen, N.]]
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[[Category: Hakulinen N]]
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[[Category: Janis, J.]]
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[[Category: Janis J]]
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[[Category: Leisola, M.]]
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[[Category: Leisola M]]
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[[Category: Rouvinen, J.]]
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[[Category: Rouvinen J]]
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[[Category: Turunen, O]]
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[[Category: Turunen O]]
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[[Category: Family 11]]
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[[Category: Glycosyl hydrolase]]
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[[Category: Thermostability]]
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[[Category: Xylanase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 02:37:19 2009''
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Current revision

Thermophilic b-1,4-xylanase from Nonomuraea flexuosa

PDB ID 1m4w

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