1qno: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(5 intermediate revisions by the same user not shown)
Line 1: Line 1:
==The 3-D structure of a Trichoderma reesei b-mannanase from glycoside hydrolase family 5==
==The 3-D structure of a Trichoderma reesei b-mannanase from glycoside hydrolase family 5==
<StructureSection load='1qno' size='340' side='right' caption='[[1qno]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1qno' size='340' side='right'caption='[[1qno]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1qno]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QNO FirstGlance]. <br>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qnp|1qnp]], [[1qnq|1qnq]], [[1qnr|1qnr]], [[1qns|1qns]]</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qno OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qno RCSB], [http://www.ebi.ac.uk/pdbsum/1qno PDBsum]</span></td></tr>
</table>
</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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qn/1qno_consurf.spt"</scriptWhenChecked>
     <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>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:10666621<ref>PMID:10666621</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Temperature value vs. resolution|Temperature value vs. resolution]]
*[[Mannosidase 3D structures|Mannosidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Mannan endo-1,4-beta-mannosidase]]
[[Category: Large Structures]]
[[Category: Trichoderma reesei]]
[[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: Anomalous scattering]]
[[Category: Hydrolase]]
[[Category: Mannanase]]

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

1qno 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 2Å
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

1qno, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1qno&oldid=4130074"