1cem: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
(12 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1cem.jpg|left|200px]]


<!--
==ENDOGLUCANASE A (CELA) CATALYTIC CORE, RESIDUES 33-395==
The line below this paragraph, containing "STRUCTURE_1cem", creates the "Structure Box" on the page.
<StructureSection load='1cem' size='340' side='right'caption='[[1cem]], [[Resolution|resolution]] 1.65&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'>[[1cem]] 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=1CEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CEM 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]] 1.65&#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=1cem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cem OCA], [https://pdbe.org/1cem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cem RCSB], [https://www.ebi.ac.uk/pdbsum/1cem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cem ProSAT]</span></td></tr>
{{STRUCTURE_1cem| PDB=1cem |  SCENE= }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/GUNA_ACET2 GUNA_ACET2] 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/1cem_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=1cem ConSurf].
<div style="clear:both"></div>


'''ENDOGLUCANASE A (CELA) CATALYTIC CORE, RESIDUES 33-395'''
==See Also==
 
*[[Glucanase 3D structures|Glucanase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
BACKGROUND. Cellulases, which catalyze the hydrolysis of glycosidic bonds in cellulose, can be classified into several different protein families. Endoglucanase CelA is a member of glycosyl hydrolase family 8, a family for which no structural information was previously available. RESULTS. The crystal structure of CelA was determined by multiple isomorphous replacement and refined to 1.65 A resolution. The protein folds into a regular (alpha/alpha)6 barrel formed by six inner and six outer alpha helices. Cello-oligosaccharides bind to an acidic cleft containing at least five D-glucosyl-binding subsites (A-E) such that the scissile glycosidic linkage lies between subsites C and D. The strictly conserved residue Glu95, which occupies the center of the substrate-binding cleft and is hydrogen bonded to the glycosidic oxygen, has been assigned the catalytic role of proton donor. CONCLUSIONS. The present analysis provides a basis for modeling homologous family 8 cellulases. The architecture of the active-site cleft, presenting at least five glucosyl-binding subsites, explains why family 8 cellulases cleave cello-oligosaccharide polymers that are at least five D-glycosyl subunits long. Furthermore, the structure of CelA allows comparison with (alpha/alpha)6 barrel glycosidases that are not related in sequence, suggesting a possible, albeit distant, evolutionary relationship between different families of glycosyl hydrolases.
[[Category: Acetivibrio thermocellus]]
 
[[Category: Large Structures]]
==About this Structure==
[[Category: Alzari PM]]
1CEM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEM OCA].
 
==Reference==
The crystal structure of endoglucanase CelA, a family 8 glycosyl hydrolase from Clostridium thermocellum., Alzari PM, Souchon H, Dominguez R, Structure. 1996 Mar 15;4(3):265-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8805535 8805535]
[[Category: Cellulase]]
[[Category: Clostridium thermocellum]]
[[Category: Single protein]]
[[Category: Alzari, P M.]]
[[Category: Cellulase]]
[[Category: Clostridium thermocellum]]
[[Category: Family d/8 of glycosyl hydrolase]]
[[Category: Glycosyl hydrolase]]
[[Category: Glycosyltransferase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:38:56 2008''

Latest revision as of 06:42, 7 February 2024

ENDOGLUCANASE A (CELA) CATALYTIC CORE, RESIDUES 33-395

1cem, resolution 1.65Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1cem&oldid=4041089"