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[[Image:1qnq.gif|left|200px]]<br />
<applet load="1qnq" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1qnq, resolution 1.65&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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?10666621 (full description)]]
<StructureSection load='1qnq' size='340' side='right'caption='[[1qnq]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1qnq]] 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=1QNQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QNQ 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]] 1.65&#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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TPT:2,2 6,2-TERPYRIDINE+PLATINUM(II)+CHLORIDE'>TPT</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=1qnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qnq OCA], [https://pdbe.org/1qnq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qnq RCSB], [https://www.ebi.ac.uk/pdbsum/1qnq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qnq 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/1qnq_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=1qnq ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1QNQ 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 NAG, SO4 and TPT 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]]. Structure known Active Site: MAN. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QNQ 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: SO4]]
[[Category: TPT]]
[[Category: anomalous scattering]]
[[Category: mannanase]]
[[Category: trichoderma reesei]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:34:05 2007''

Latest revision as of 09:05, 17 April 2024

The 3-D structure of a Trichoderma reesei b-mannanase from glycoside hydrolase family 5The 3-D structure of a Trichoderma reesei b-mannanase from glycoside hydrolase family 5

Structural highlights

1qnq is a 1 chain structure with sequence from Trichoderma reesei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.65Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).[1] [2] [3] [PROSITE-ProRule:PRU00597][SAM:MobiDB-lite][4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Rosengren A, Reddy SK, Sjöberg JS, Aurelius O, Logan DT, Kolenová K, Stålbrand H. An Aspergillus nidulans β-mannanase with high transglycosylation capacity revealed through comparative studies within glycosidase family 5. Appl Microbiol Biotechnol. 2014 Dec;98(24):10091-104. PMID:24950755 doi:10.1007/s00253-014-5871-8
  2. ↑ Stålbrand H, Saloheimo A, Vehmaanperä J, Henrissat B, Penttilä M. Cloning and expression in Saccharomyces cerevisiae of a Trichoderma reesei beta-mannanase gene containing a cellulose binding domain. Appl Environ Microbiol. 1995 Mar;61(3):1090-7. PMID:7793911 doi:10.1128/aem.61.3.1090-1097.1995
  3. ↑ Harjunpää V, Teleman A, Siika-Aho M, Drakenberg T. Kinetic and stereochemical studies of manno-oligosaccharide hydrolysis catalysed by beta-mannanases from Trichoderma reesei. Eur J Biochem. 1995 Nov 15;234(1):278-83. PMID:8529653 doi:10.1111/j.1432-1033.1995.278_c.x
  4. ↑ Rosengren A, Reddy SK, Sjöberg JS, Aurelius O, Logan DT, Kolenová K, Stålbrand H. An Aspergillus nidulans β-mannanase with high transglycosylation capacity revealed through comparative studies within glycosidase family 5. Appl Microbiol Biotechnol. 2014 Dec;98(24):10091-104. PMID:24950755 doi:10.1007/s00253-014-5871-8

1qnq, resolution 1.65Å

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