1qno: Difference between revisions

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-[[Image:1qno.gif|left|200px]]<br /><applet load="1qno" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1qno, resolution 2.00&Aring;" />
-'''THE 3-D STRUCTURE OF A TRICHODERMA REESEI B-MANNANASE FROM GLYCOSIDE HYDROLASE FAMILY 5'''<br />
-==Overview==
+==The 3-D structure of a Trichoderma reesei b-mannanase from glycoside hydrolase family 5==
-The crystal structure of the catalytic core domain of beta-mannanase from the fungus Trichoderma reesei has been determined at a resolution of 1.5 A. The structure was solved using the anomalous scattering from a single non-isomorphous platinum complex with two heavy-metal sites in space group P2(1). The map computed with the experimental phases was enhanced by the application of an automated model building and refinement procedure using the amplitudes and experimental phases as observations. This approach is expected to be of more general application. The structure of the native enzyme and complexes with Tris-HCl and mannobiose are also reported: the mannobiose binds in subsites +1 and +2. The structure is briefly compared with that of the homologous beta-mannanase from the bacterium Thermomonospora fusca.
+<StructureSection load='1qno' size='340' side='right'caption='[[1qno]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1qno]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QNO FirstGlance]. <br>
+</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&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qno OCA], [https://pdbe.org/1qno PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qno RCSB], [https://www.ebi.ac.uk/pdbsum/1qno PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qno ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MANA_HYPJR MANA_HYPJR] Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Active against locust bean gum and ivory nut mannan, releasing mainly tri- and disaccharides (PubMed:7793911, Ref.3, Ref.4, PubMed:8529653). Also has transglycosylation activity. Transglycosylation of two mannotrioses into a mannohexaose is the major transglycosylation route (PubMed:8529653, Ref.7, PubMed:24950755).<ref>PMID:24950755</ref> <ref>PMID:7793911</ref> <ref>PMID:8529653</ref> [PROSITE-ProRule:PRU00597][SAM:MobiDB-lite]<ref>PMID:24950755</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qn/1qno_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1qno ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-QNO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] Known structural/functional Site: <scene name='pdbsite=MAN:Mannan+Binding+Site'>MAN</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNO OCA].
+*[[Mannosidase 3D structures|Mannosidase 3D structures]]
+== References ==
-==Reference==
+<references/>
-The three-dimensional structure of a Trichoderma reesei beta-mannanase from glycoside hydrolase family 5., Sabini E, Schubert H, Murshudov G, Wilson KS, Siika-Aho M, Penttila M, Acta Crystallogr D Biol Crystallogr. 2000 Jan;56(Pt 1):3-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10666621 10666621]
+__TOC__
-[[Category: Hypocrea jecorina]]
+</StructureSection>
-[[Category: Mannan endo-1,4-beta-mannosidase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Trichoderma reesei]]
-[[Category: Murshudov, G.]]
+[[Category: Murshudov G]]
-[[Category: Penttila, M.]]
+[[Category: Penttila M]]
-[[Category: Sabini, E.]]
+[[Category: Sabini E]]
-[[Category: Schubert, H.]]
+[[Category: Schubert H]]
-[[Category: Siika-Aho, M.]]
+[[Category: Siika-Aho M]]
-[[Category: Wilson, K S.]]
+[[Category: Wilson KS]]
-[[Category: NAG]]
-[[Category: TRS]]
-[[Category: anomalous scattering]]
-[[Category: mannanase]]
-[[Category: trichoderma reesei]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:41:41 2008''