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.


1ovw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:09, 3 April 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1ovw.jpg|left|200px]]<br /><applet load="1ovw" size="350" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1ovw, resolution 2.7&Aring;" />
 
-
'''ENDOGLUCANASE I COMPLEXED WITH NON-HYDROLYSABLE SUBSTRATE ANALOGUE'''<br />
 
-
==Overview==
+
==ENDOGLUCANASE I COMPLEXED WITH NON-HYDROLYSABLE SUBSTRATE ANALOGUE==
-
Endoglucanase I (EG I) is a cellulase, from glycosyl hydrolase family 7, which cleaves the beta-1,4 linkages of cellulose with overall retention of configuration. The structure of the EG I from Fusarium oxysproum, complexed to a nonhydrolyzable thiooligosaccharide substrate analogue, has been determined by X-ray crystallography at a resolution of 2.7 A utilizing the 4-fold noncrystallographic symmetry present in the asymmetric unit. The electron density map clearly reveals the presence of three glucosyl units of the inhibitor, consistent with the known number of sugar-binding subsites, located at the active site of the enzyme in the -2, -1, and +1 subsites, i.e., actually spanning the point of enzymatic cleavage. The pyranose ring at the point of potential enzymatic cleavage is clearly distorted from the standard 4C1 chair as was originally suggested for beta-retaining enzymes by Phillips [Ford, L.O., Johnson, L.N., Machin, P. A., Phillips, D.C., &amp; Tijan, T. (1974) J. Mol. Biol, 88, 349-371]. The distortion observed goes beyond the "sofa" conformation observed in previous studies and results in a conformation whose salient feature is the resulting quasi-axial orientation for the glycosidic bond and leaving group, as predicted by stereoelectronic theory. An almost identical conformation has recently been observed in a complex of chitobiase with its unhydrolyzed substrate [Tews, I., Perrakis, A., Oppenheim, A., Dauter, Z., Wilson, K. S., &amp; Vorgias, C. E. (1996) Nat. Struct. Biol. 3, 638-648]. The striking similarity between these two complexes extends beyond the almost identical pyranose ring distortion. The overlap of the two respective sugars places the enzymatic nucleophile of endoglucanase I in coincidence with the C2 acetamido oxygen of N-acetylglucosamine in the catalytic site of the chitobiase, substantiating the involvement of this group in the catalytic mechanism of chitobiase and related chitinolytic enzymes. The endoglucanase I complex with the thiosaccharide substrate analogue clearly illustrates the potential of nonhydrolyzable sulfur-linked oligosaccharides in the elucidation of substrate binding and catalysis by glycosyl hydrolases.
+
<StructureSection load='1ovw' size='340' side='right'caption='[[1ovw]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1ovw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OVW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OVW FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</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=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PRD_900097:4-thio-beta-D-glucopyranosyl-(1- 4)-4-thio-beta-D-glucopyranosyl-(1- 4)-1,4-dithio-beta-D-glucopyranose'>PRD_900097</scene>, <scene name='pdbligand=SGC:4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE'>SGC</scene>, <scene name='pdbligand=SSG:1,4-DEOXY-1,4-DITHIO-BETA-D-GLUCOPYRANOSE'>SSG</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=1ovw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ovw OCA], [https://pdbe.org/1ovw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ovw RCSB], [https://www.ebi.ac.uk/pdbsum/1ovw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ovw ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/GUNC_FUSOX GUNC_FUSOX]
 +
== 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/ov/1ovw_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=1ovw ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1OVW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_oxysporum Fusarium oxysporum] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=DP5:'>DP5</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] Known structural/functional Sites: <scene name='pdbsite=CTA:Dp5+Binding+Site'>CTA</scene>, <scene name='pdbsite=CTB:Dp5+Binding+Site'>CTB</scene>, <scene name='pdbsite=CTC:Dp5+Binding+Site'>CTC</scene> and <scene name='pdbsite=CTD:Dp5+Binding+Site'>CTD</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OVW OCA].
+
*[[Glucanase 3D structures|Glucanase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Structure of the Fusarium oxysporum endoglucanase I with a nonhydrolyzable substrate analogue: substrate distortion gives rise to the preferred axial orientation for the leaving group., Sulzenbacher G, Driguez H, Henrissat B, Schulein M, Davies GJ, Biochemistry. 1996 Dec 3;35(48):15280-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8952478 8952478]
+
-
[[Category: Cellulase]]
+
[[Category: Fusarium oxysporum]]
[[Category: Fusarium oxysporum]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Davies, G J.]]
+
[[Category: Davies GJ]]
-
[[Category: Schulein, M.]]
+
[[Category: Schulein M]]
-
[[Category: Sulzenbacher, G.]]
+
[[Category: Sulzenbacher G]]
-
[[Category: DP5]]
+
-
[[Category: NAG]]
+
-
[[Category: cellulose degradation]]
+
-
[[Category: glycoprotein]]
+
-
[[Category: glycosidase]]
+
-
[[Category: hydrolase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:15 2008''
+

Current revision

ENDOGLUCANASE I COMPLEXED WITH NON-HYDROLYSABLE SUBSTRATE ANALOGUE

PDB ID 1ovw

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/1ovw"
Personal tools