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.

2fuz

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:24, 20 June 2018

UGL hexagonal crystal structure without glycine and DTT molecules

Structural highlights

2fuz is a 1 chain structure with sequence from Bacgl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2fv0, 2fv1
Gene:	ugl (BACGL)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[UGL_BACGL] Catalyzes the hydrolysis of oligosaccharides with unsaturated glucuronyl residues at the non-reducing terminal, to a sugar or an amino sugar, and an unsaturated D-glucuronic acid (GlcA), which is nonenzymatically converted immediately to alpha-keto acid.^[1] ^[2]

Evolutionary Conservation

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

Publication Abstract from PubMed

Bacterial unsaturated glucuronyl hydrolases (UGLs) together with polysaccharide lyases are responsible for the complete depolymerization of mammalian extracellular matrix glycosaminoglycans. UGL acts on various oligosaccharides containing unsaturated glucuronic acid (DeltaGlcA) at the nonreducing terminus and releases DeltaGlcA through hydrolysis. In this study, we demonstrate the substrate recognition mechanism of the UGL of Bacillus sp. GL1 by determining the X-ray crystallographic structure of its substrate-enzyme complexes. The tetrasaccharide-enzyme complex demonstrated that at least four subsites are present in the active pocket. Although several amino acid residues are crucial for substrate binding, the enzyme strongly recognizes DeltaGlcA at subsite -1 through the formation of hydrogen bonds and stacking interactions, and prefers N-acetyl-d-galactosamine and glucose rather than N-acetyl-d-glucosamine as a residue accommodated in subsite +1, due to the steric hindrance.

Substrate recognition by unsaturated glucuronyl hydrolase from Bacillus sp. GL1.,Itoh T, Hashimoto W, Mikami B, Murata K Biochem Biophys Res Commun. 2006 May 26;344(1):253-62. PMID:16630576^[3]

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

References

↑ Hashimoto W, Kobayashi E, Nankai H, Sato N, Miya T, Kawai S, Murata K. Unsaturated glucuronyl hydrolase of Bacillus sp. GL1: novel enzyme prerequisite for metabolism of unsaturated oligosaccharides produced by polysaccharide lyases. Arch Biochem Biophys. 1999 Aug 15;368(2):367-74. PMID:10441389 doi:http://dx.doi.org/10.1006/abbi.1999.1305
↑ Nakamichi Y, Maruyama Y, Mikami B, Hashimoto W, Murata K. Structural determinants in streptococcal unsaturated glucuronyl hydrolase for recognition of glycosaminoglycan sulfate groups. J Biol Chem. 2011 Feb 25;286(8):6262-71. Epub 2010 Dec 8. PMID:21147778 doi:10.1074/jbc.M110.182618
↑ Itoh T, Hashimoto W, Mikami B, Murata K. Substrate recognition by unsaturated glucuronyl hydrolase from Bacillus sp. GL1. Biochem Biophys Res Commun. 2006 May 26;344(1):253-62. PMID:16630576 doi:10.1016/j.bbrc.2006.03.141

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2fuz"

@@ Line 1: / Line 1: @@
 ==UGL hexagonal crystal structure without glycine and DTT molecules==
 <StructureSection load='2fuz' size='340' side='right' caption='[[2fuz]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fv0|2fv0]], [[2fv1|2fv1]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ugl ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=84635 BACGL])</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=2fuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fuz OCA], [http://pdbe.org/2fuz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fuz RCSB], [http://www.ebi.ac.uk/pdbsum/2fuz PDBsum]</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=2fuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fuz OCA], [http://pdbe.org/2fuz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fuz RCSB], [http://www.ebi.ac.uk/pdbsum/2fuz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fuz ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fu/2fuz_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fu/2fuz_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2fuz

From Proteopedia

Revision as of 07:24, 20 June 2018

UGL hexagonal crystal structure without glycine and DTT molecules

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox