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1rh9

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(New page: 200px<br /><applet load="1rh9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rh9, resolution 1.50&Aring;" /> '''Family GH5 endo-beta...)
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[[Image:1rh9.gif|left|200px]]<br /><applet load="1rh9" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1rh9, resolution 1.50&Aring;" />
 
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'''Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)'''<br />
 
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==Overview==
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==Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)==
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The three-dimensional crystal structure of tomato (Lycopersicon, esculentum) beta-mannanase 4a (LeMAN4a) has been determined to 1.5 A, resolution. The enzyme adopts the (beta/alpha)(8) fold common to the, members of glycohydrolase family GH5. The structure is comparable with, those of the homologous Trichoderma reesei and Thermomonospora fusca, beta-mannanases: There is a conserved three-stranded beta-sheet located, near the N terminus that stacks against the central beta-barrel at the end, opposite the active site. Three noncanonical beta-helices surround the, active site. Similar helices are found in T. reesei but not T. fusca, beta-mannanase. By analogy with other beta-mannanases, the catalytic, acid/base residue is E204 and the nucleophile residue is E318. The active, site cleft of L. esculentum beta-mannanase most closely resembles that of, the T. reesei isozyme. A model of substrate binding in LeMAN4a is proposed, in which the mannosyl residue occupying the -1 subsite of the enzyme, adopts the (1)S(5) skew-boat conformation.
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<StructureSection load='1rh9' size='340' side='right'caption='[[1rh9]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1rh9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RH9 FirstGlance]. <br>
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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]] 1.5&#8491;</td></tr>
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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=1rh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rh9 OCA], [https://pdbe.org/1rh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rh9 RCSB], [https://www.ebi.ac.uk/pdbsum/1rh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rh9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MAN4_SOLLC MAN4_SOLLC] Possesses endo-beta-mannanase and mannan transglycosylase activities. May be involved in cell wall degradation during fruit ripening.<ref>PMID:12427992</ref> <ref>PMID:16649044</ref>
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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/rh/1rh9_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=1rh9 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 three-dimensional crystal structure of tomato (Lycopersicon esculentum) beta-mannanase 4a (LeMAN4a) has been determined to 1.5 A resolution. The enzyme adopts the (beta/alpha)(8) fold common to the members of glycohydrolase family GH5. The structure is comparable with those of the homologous Trichoderma reesei and Thermomonospora fusca beta-mannanases: There is a conserved three-stranded beta-sheet located near the N terminus that stacks against the central beta-barrel at the end opposite the active site. Three noncanonical beta-helices surround the active site. Similar helices are found in T. reesei but not T. fusca beta-mannanase. By analogy with other beta-mannanases, the catalytic acid/base residue is E204 and the nucleophile residue is E318. The active site cleft of L. esculentum beta-mannanase most closely resembles that of the T. reesei isozyme. A model of substrate binding in LeMAN4a is proposed in which the mannosyl residue occupying the -1 subsite of the enzyme adopts the (1)S(5) skew-boat conformation.
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==About this Structure==
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Three-dimensional structure of (1,4)-beta-D-mannan mannanohydrolase from tomato fruit.,Bourgault R, Oakley AJ, Bewley JD, Wilce MC Protein Sci. 2005 May;14(5):1233-41. PMID:15840830<ref>PMID:15840830</ref>
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1RH9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum]. 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RH9 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Three-dimensional structure of (1,4)-beta-D-mannan mannanohydrolase from tomato fruit., Bourgault R, Oakley AJ, Bewley JD, Wilce MC, Protein Sci. 2005 May;14(5):1233-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15840830 15840830]
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</div>
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[[Category: Mannan endo-1,4-beta-mannosidase]]
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<div class="pdbe-citations 1rh9" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Solanum lycopersicum]]
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[[Category: Bewley, J.D.]]
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[[Category: Bourgault, R.]]
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[[Category: Oakley, A.J.]]
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[[Category: Wilce, M.C.J.]]
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[[Category: endo-beta-mannase]]
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[[Category: glycoside hydrolase family 5]]
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[[Category: mannan]]
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[[Category: retaining]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:35:53 2007''
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==See Also==
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*[[Mannosidase 3D structures|Mannosidase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Solanum lycopersicum]]
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[[Category: Bewley JD]]
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[[Category: Bourgault R]]
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[[Category: Oakley AJ]]
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[[Category: Wilce MCJ]]

Current revision

Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)

PDB ID 1rh9

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