2fuz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:45, 25 October 2023) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2fuz.png|left|200px]]
 
-
<!--
+
==UGL hexagonal crystal structure without glycine and DTT molecules==
-
The line below this paragraph, containing "STRUCTURE_2fuz", creates the "Structure Box" on the page.
+
<StructureSection load='2fuz' size='340' side='right'caption='[[2fuz]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2fuz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._GL1 Bacillus sp. GL1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FUZ FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
-
{{STRUCTURE_2fuz| PDB=2fuz | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fuz OCA], [https://pdbe.org/2fuz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fuz RCSB], [https://www.ebi.ac.uk/pdbsum/2fuz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fuz ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/UGL_BACGL 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.<ref>PMID:10441389</ref> <ref>PMID:21147778</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/fu/2fuz_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=2fuz ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
===UGL hexagonal crystal structure without glycine and DTT molecules===
+
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<ref>PMID:16630576</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_16630576}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 2fuz" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 16630576 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_16630576}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Bacillus sp. GL1]]
-
2FUZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUZ OCA].
+
[[Category: Large Structures]]
-
 
+
[[Category: Hashimoto W]]
-
==Reference==
+
[[Category: Itoh T]]
-
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:[http://www.ncbi.nlm.nih.gov/pubmed/16630576 16630576]
+
[[Category: Mikami B]]
-
[[Category: Bacillus sp.]]
+
[[Category: Murata K]]
-
[[Category: Single protein]]
+
-
[[Category: Hashimoto, W.]]
+
-
[[Category: Itoh, T.]]
+
-
[[Category: Mikami, B.]]
+
-
[[Category: Murata, K.]]
+
-
[[Category: Alpha6/alpha6-barrel]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:05:17 2008''
+

Current revision

UGL hexagonal crystal structure without glycine and DTT molecules

PDB ID 2fuz

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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