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1cx1

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Revision as of 08:12, 12 December 2018

SECOND N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI BETA-1,4-GLUCANASE C, NMR, 22 STRUCTURES

Structural highlights

1cx1 is a 1 chain structure with sequence from "bacterium_fimi"_mcbeth_and_scales_1913 "bacterium fimi" mcbeth and scales 1913. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1ulo, 1ulp
Activity:	Cellulase, with EC number 3.2.1.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GUNC_CELFA] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

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

The 1,4-beta-glucanase CenC from Cellulomonas fimi contains two cellulose-binding domains, CBD(N1) and CBD(N2), arranged in tandem at its N-terminus. These homologous CBDs are distinct in their selectivity for binding amorphous and not crystalline cellulose. Multidimensional heteronuclear nuclear magnetic resonance (NMR) spectroscopy was used to determine the tertiary structure of CBD(N2) in the presence of saturating amounts of cellopentaose. A total of 1996 experimental restraints were used to calculate an ensemble of 21 final structures for the protein. CBD(Nu2) is composed of 11 beta-strands, folded into two antiparallel beta-sheets, with a topology of a jellyroll beta-sandwich. On the basis of patterns of chemical shift perturbations accompanying the addition of cellooligosaccharides, as well as the observation of intermolecular protein-sugar NOE interactions, the cellulose-binding site of CBD(N2) was identified as a cleft that lies across one face of the beta-sandwich. The thermodynamic basis for the binding of cellooligosaccharides was investigated using isothermal titration calorimetry and NMR spectroscopy. Binding is enthalpically driven and consistent with a structural model involving hydrogen bonding between the equatorial hydroxyls of the glucopyranosyl rings and polar amino acid side chains lining the CBD(N2) cleft. Affinity electrophoresis was used to determine that CBD(N2) also binds soluble beta-1,4-linked polymers of glucose, including hydroxyethylcellulose and beta-1,3-1,4-glucans. This study complements a previous analysis of CBD(N1) [Johnson, P. E., Joshi, M. D., Tomme, P., Kilburn, D. G., and McIntosh, L. P. (1996) Biochemistry 35, 14381-14394] and demonstrates that the homologous CBDs from CenC share very similar structures and sugar binding properties.

Structure and binding specificity of the second N-terminal cellulose-binding domain from Cellulomonas fimi endoglucanase C.,Brun E, Johnson PE, Creagh AL, Tomme P, Webster P, Haynes CA, McIntosh LP Biochemistry. 2000 Mar 14;39(10):2445-58. PMID:10704194^[1]

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

References

↑ Brun E, Johnson PE, Creagh AL, Tomme P, Webster P, Haynes CA, McIntosh LP. Structure and binding specificity of the second N-terminal cellulose-binding domain from Cellulomonas fimi endoglucanase C. Biochemistry. 2000 Mar 14;39(10):2445-58. PMID:10704194

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cx1"

@@ Line 3: / Line 3: @@
 <StructureSection load='1cx1' size='340' side='right' caption='[[1cx1]], [[NMR_Ensembles_of_Models | 22 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1cx1]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CX1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CX1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1cx1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_fimi"_mcbeth_and_scales_1913 "bacterium fimi" mcbeth and scales 1913]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CX1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CX1 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ulo|1ulo]], [[1ulp|1ulp]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
@@ Line 14: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cx/1cx1_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cx/1cx1_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 36: / Line 36: @@
 __TOC__
 </StructureSection>
+[[Category: Bacterium fimi mcbeth and scales 1913]]
 [[Category: Cellulase]]
 [[Category: Brun, E]]

1cx1

From Proteopedia

Revision as of 08:12, 12 December 2018

SECOND N-TERMINAL CELLULOSE-BINDING DOMAIN FROM CELLULOMONAS FIMI BETA-1,4-GLUCANASE C, NMR, 22 STRUCTURES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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