1h1a

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{{Seed}}
 
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[[Image:1h1a.png|left|200px]]
 
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==Thermophilic beta-1,4-xylanase from Chaetomium thermophilum==
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The line below this paragraph, containing "STRUCTURE_1h1a", creates the "Structure Box" on the page.
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<StructureSection load='1h1a' size='340' side='right'caption='[[1h1a]], [[Resolution|resolution]] 1.75&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'>[[1h1a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H1A 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]] 1.75&#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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1h1a| PDB=1h1a | 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=1h1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h1a OCA], [https://pdbe.org/1h1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h1a RCSB], [https://www.ebi.ac.uk/pdbsum/1h1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h1a ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8J1V6_9PEZI Q8J1V6_9PEZI]
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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/h1/1h1a_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=1h1a 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 CHAETOMIUM THERMOPHILUM===
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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 1h1a" 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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1H1A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1A OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12653995 12653995]
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[[Category: Chaetomium thermophilum]]
[[Category: Chaetomium thermophilum]]
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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: Hakulinen N]]
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[[Category: Hakulinen, N.]]
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[[Category: Rouvinen J]]
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[[Category: Rouvinen, J.]]
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[[Category: Family 11]]
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[[Category: Glycosyl hydrolase]]
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[[Category: Thermostability glycosidase]]
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[[Category: Xylanase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:27:17 2008''
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Current revision

Thermophilic beta-1,4-xylanase from Chaetomium thermophilum

PDB ID 1h1a

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