This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4cd5

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 17:39, 7 September 2022

The structure of GH26 beta-mannanase CjMan26C from Cellvibrio japonicus in complex with ManMIm

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4cd5"

@@ Line 3: / Line 3: @@
 <StructureSection load='4cd5' size='340' side='right'caption='[[4cd5]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4cd5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Celju Celju]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CD5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CD5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4cd5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellvibrio_japonicus_Ueda107 Cellvibrio japonicus Ueda107]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CD5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CD5 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MVL:(5R,6R,7S,8R)-5-(HYDROXYMETHYL)-5,6,7,8-TETRAHYDROIMIDAZO[1,2-A]PYRIDINE-6,7,8-TRIOL'>MVL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MVL:(5R,6R,7S,8R)-5-(HYDROXYMETHYL)-5,6,7,8-TETRAHYDROIMIDAZO[1,2-A]PYRIDINE-6,7,8-TRIOL'>MVL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cd4|4cd4]], [[4cd6|4cd6]], [[4cd7|4cd7]], [[4cd8|4cd8]]</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=4cd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cd5 OCA], [https://pdbe.org/4cd5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cd5 RCSB], [https://www.ebi.ac.uk/pdbsum/4cd5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cd5 ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cd5 OCA], [http://pdbe.org/4cd5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cd5 RCSB], [http://www.ebi.ac.uk/pdbsum/4cd5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cd5 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[[https://www.uniprot.org/uniprot/B3PGI1_CELJU B3PGI1_CELJU]]
-Mannosidases catalyze the hydrolysis of a diverse range of polysaccharides and glycoconjugates, and the various sequence-based mannosidase families have evolved ingenious strategies to overcome the stereoelectronic challenges of mannoside chemistry. Using a combination of computational chemistry, inhibitor design and synthesis, and X-ray crystallography of inhibitor/enzyme complexes, it is demonstrated that mannoimidazole-type inhibitors are energetically poised to report faithfully on mannosidase transition-state conformation, and provide direct evidence for the conformational itinerary used by diverse mannosidases, including beta-mannanases from families GH26 and GH113. Isofagomine-type inhibitors are poor mimics of transition-state conformation, owing to the high energy barriers that must be crossed to attain mechanistically relevant conformations, however, these sugar-shaped heterocycles allow the acquisition of ternary complexes that span the active site, thus providing valuable insight into active-site residues involved in substrate recognition.
-Combined inhibitor free-energy landscape and structural analysis reports on the mannosidase conformational coordinate.,Williams RJ, Iglesias-Fernandez J, Stepper J, Jackson A, Thompson AJ, Lowe EC, White JM, Gilbert HJ, Rovira C, Davies GJ, Williams SJ Angew Chem Int Ed Engl. 2014 Jan 20;53(4):1087-91. doi: 10.1002/anie.201308334., Epub 2013 Dec 11. PMID:24339341<ref>PMID:24339341</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4cd5" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Celju]]
+[[Category: Cellvibrio japonicus Ueda107]]
 [[Category: Large Structures]]
-[[Category: Mannan endo-1,4-beta-mannosidase]]
+[[Category: Davies GJ]]
-[[Category: Davies, G J]]
+[[Category: Gilbert HJ]]
-[[Category: Gilbert, H J]]
+[[Category: Iglesias-Fernandez J]]
-[[Category: Iglesias-Fernandez, J]]
+[[Category: Jackson A]]
-[[Category: Jackson, A]]
+[[Category: Lowe EC]]
-[[Category: Lowe, E C]]
+[[Category: Rovira C]]
-[[Category: Rovira, C]]
+[[Category: Stepper J]]
-[[Category: Stepper, J]]
+[[Category: Thompson AJ]]
-[[Category: Thompson, A J]]
+[[Category: White JM]]
-[[Category: White, J M]]
+[[Category: Williams RJ]]
-[[Category: Williams, R J]]
+[[Category: Williams SJ]]
-[[Category: Williams, S J]]
-[[Category: Beta-mannosidase]]
-[[Category: Biocatalysis]]
-[[Category: Cazy]]
-[[Category: Conformation]]
-[[Category: Enzyme-carbohydrate interaction]]
-[[Category: Gh113]]
-[[Category: Gh26]]
-[[Category: Glycosidase inhibition]]
-[[Category: Glycoside hydrolase]]
-[[Category: Hydrolase]]
-[[Category: Mannose]]
-[[Category: Mannosidase]]
-[[Category: Quantum mechanic]]

4cd5

From Proteopedia

Revision as of 17:39, 7 September 2022

The structure of GH26 beta-mannanase CjMan26C from Cellvibrio japonicus in complex with ManMIm

Structural highlights

Function

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox