1cec

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1cec" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cec, resolution 2.15&Aring;" /> '''A COMMON PROTEIN FOL...)
Current revision (06:42, 7 February 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1cec.gif|left|200px]]<br /><applet load="1cec" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1cec, resolution 2.15&Aring;" />
 
-
'''A COMMON PROTEIN FOLD AND SIMILAR ACTIVE SITE IN TWO DISTINCT FAMILIES OF BETA-GLYCANASES'''<br />
 
-
==Overview==
+
==A COMMON PROTEIN FOLD AND SIMILAR ACTIVE SITE IN TWO DISTINCT FAMILIES OF BETA-GLYCANASES==
-
The structure of Clostridium thermocellum endoglucanase CelC, a member of, the largest cellulase family (family A), has been determined at 2.15 A, resolution. The protein folds into an (alpha/beta)8 barrel, with a deep, active-site cleft generated by the insertion of a helical subdomain. The, structure of the catalytic core of xylanase XynZ, which belongs to, xylanase family F, has been determined at 1.4 A resolution. In spite of, significant differences in substrate specificity and structure (including, the absence of the helical subdomain), the general polypeptide folding, pattern, architecture of the active site and catalytic mechanism of XynZ, and CelC are similar, suggesting a common evolutionary origin.
+
<StructureSection load='1cec' size='340' side='right'caption='[[1cec]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1cec]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CEC 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]] 2.15&#8491;</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=1cec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cec OCA], [https://pdbe.org/1cec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cec RCSB], [https://www.ebi.ac.uk/pdbsum/1cec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cec ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/GUNC_ACETH GUNC_ACETH] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
 +
== 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/ce/1cec_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=1cec ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1CEC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]. 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CEC OCA].
+
*[[Glucanase 3D structures|Glucanase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
A common protein fold and similar active site in two distinct families of beta-glycanases., Dominguez R, Souchon H, Spinelli S, Dauter Z, Wilson KS, Chauvaux S, Beguin P, Alzari PM, Nat Struct Biol. 1995 Jul;2(7):569-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7664125 7664125]
+
[[Category: Acetivibrio thermocellus]]
-
[[Category: Cellulase]]
+
[[Category: Large Structures]]
-
[[Category: Clostridium thermocellum]]
+
[[Category: Alzari PM]]
-
[[Category: Single protein]]
+
[[Category: Dominguez R]]
-
[[Category: Alzari, P.M.]]
+
-
[[Category: Dominguez, R.]]
+
-
[[Category: cellulase]]
+
-
[[Category: clostridium thermocellum]]
+
-
[[Category: endoglucanase c]]
+
-
[[Category: family a/5 of cellulases/glycosyl hydrolases]]
+
-
[[Category: glycosyl hydrolase]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:22:56 2007''
+

Current revision

A COMMON PROTEIN FOLD AND SIMILAR ACTIVE SITE IN TWO DISTINCT FAMILIES OF BETA-GLYCANASES

PDB ID 1cec

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/1cec"
Personal tools