4awe: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4awe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_sitophila Neurospora sitophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AWE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AWE FirstGlance]. <br>
<table><tr><td colspan='2'>[[4awe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_sitophila Neurospora sitophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AWE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AWE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <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]] 1.4&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Mannan_endo-1,4-beta-mannosidase Mannan endo-1,4-beta-mannosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.78 3.2.1.78] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <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=4awe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4awe OCA], [https://pdbe.org/4awe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4awe RCSB], [https://www.ebi.ac.uk/pdbsum/4awe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4awe ProSAT]</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=4awe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4awe OCA], [https://pdbe.org/4awe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4awe RCSB], [https://www.ebi.ac.uk/pdbsum/4awe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4awe ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I4IY26_NEUSI I4IY26_NEUSI]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mannan endo-1,4-beta-mannosidase]]
[[Category: Neurospora sitophila]]
[[Category: Neurospora sitophila]]
[[Category: Bento, I]]
[[Category: Bento I]]
[[Category: Goncalves, A M.D]]
[[Category: De Sanctis D]]
[[Category: Sanctis, D De]]
[[Category: Goncalves AMD]]
[[Category: Silva, C S]]
[[Category: Silva CS]]
[[Category: Endo-mannanase]]
[[Category: Gh5]]
[[Category: Glycosyl hydrolase]]
[[Category: Hydrolase]]

Latest revision as of 14:37, 20 December 2023

The Crystal Structure of Chrysonilia sitophila endo-beta-D-1,4- mannanaseThe Crystal Structure of Chrysonilia sitophila endo-beta-D-1,4- mannanase

Structural highlights

4awe is a 1 chain structure with sequence from Neurospora sitophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.4Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

I4IY26_NEUSI

Publication Abstract from PubMed

The crystal structure of wild-type endo-beta-D-1,4-mannanase (EC 3.2.1.78) from the ascomycete Chrysonilia sitophila (CsMan5) has been solved at 1.40 A resolution. The enzyme isolated directly from the source shows mixed activity as both an endo-glucanase and an endo-mannanase. CsMan5 adopts the (beta/alpha)(8)-barrel fold that is well conserved within the GH5 family and has highest sequence and structural homology to the GH5 endo-mannanases. Superimposition with proteins of this family shows a unique structural arrangement of three surface loops of CsMan5 that stretch over the active centre, promoting an altered topography of the binding cleft. The most relevant feature results from the repositioning of a long loop at the extremity of the binding cleft, resulting in a shortened glycone-binding region with two subsites. The other two extended loops flanking the binding groove produce a narrower cleft compared with the wide architecture observed in GH5 homologues. Two aglycone subsites (+1 and +2) are identified and a nonconserved tryptophan (Trp271) at the +1 subsite may offer steric hindrance. Taken together, these findings suggest that the discrimination of mannan substrates is achieved through modified loop length and structure.

Endo-beta-D-1,4-mannanase from Chrysonilia sitophila displays a novel loop arrangement for substrate selectivity.,Goncalves AM, Silva CS, Madeira TI, Coelho R, de Sanctis D, San Romao MV, Bento I Acta Crystallogr D Biol Crystallogr. 2012 Nov;68(Pt 11):1468-78. doi:, 10.1107/S0907444912034646. Epub 2012 Oct 18. PMID:23090396[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Goncalves AM, Silva CS, Madeira TI, Coelho R, de Sanctis D, San Romao MV, Bento I. Endo-beta-D-1,4-mannanase from Chrysonilia sitophila displays a novel loop arrangement for substrate selectivity. Acta Crystallogr D Biol Crystallogr. 2012 Nov;68(Pt 11):1468-78. doi:, 10.1107/S0907444912034646. Epub 2012 Oct 18. PMID:23090396 doi:http://dx.doi.org/10.1107/S0907444912034646

4awe, resolution 1.40Å

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OCA