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1cnv

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(New page: 200px<br /><applet load="1cnv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cnv, resolution 1.65&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1cnv.gif|left|200px]]<br /><applet load="1cnv" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cnv, resolution 1.65&Aring;" />
 
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'''CRYSTAL STRUCTURE OF CONCANAVALIN B AT 1.65 A RESOLUTION'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF CONCANAVALIN B AT 1.65 A RESOLUTION==
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Seeds of Canavalia ensiformis (jack bean) contain besides large amounts of, canavalin and concanavalin A, a protein with a molecular mass of 33,800, which has been named concanavalin B. Although concanavalin B shares about, 40% sequence identity with plant chitinases belonging to glycosyl, hydrolase family 18, no chitinase activity could be detected for this, protein. To resolve this incongruity concanavalin B was crystallised and, its three-dimensional structure determined at 1.65 A (1 A = 0.1 nm), resolution. The structure consists of a single domain with a (beta/alpha)8, topology. A 30 amino acid residue long loop occurs between the second, beta-strand of the barrel and the second alpha-helix. This extended loop, is unusual for the (beta/alpha)8 topology, but appears in a similar, conformation in the structures of the seed protein narbonin and several, chitinases as well. Two non-proline cis-peptide bonds are present in the, structure of concanavalin B: Ser34-Phe, and Trp265-Asn. This structural, feature is rarely observed in proteins, but could also be identified in, the three-dimensional structures of family 18 chitinases and narbonin in, coincident positions. In the chitinases the aromatic residues of the, non-proline cis-peptides have been proposed to have a function in the, binding of the substrate. The region in concanavalin B, where in, chitinases the active site is located, shows two significant differences., First, the catalytic glutamic acid is a glutamine in concanavalin B., Second, although part of the substrate binding cleft of the chitinases is, present in concanavalin B, it is much shorter. From this we conclude that, concanavalin B and family 18 chitinases are closely related, but that, concanavalin B has lost its enzymatic function. It still may act as a, carbohydrate binding protein, however.
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<StructureSection load='1cnv' size='340' side='right'caption='[[1cnv]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cnv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CNV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CNV FirstGlance]. <br>
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</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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cnv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cnv OCA], [https://pdbe.org/1cnv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cnv RCSB], [https://www.ebi.ac.uk/pdbsum/1cnv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cnv ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CONB_CANEN CONB_CANEN] May act as a carbohydrate-binding protein.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cn/1cnv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1cnv ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1CNV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CNV OCA].
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*[[Concanavalin 3D structures|Concanavalin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of concanavalin B at 1.65 A resolution. An "inactivated" chitinase from seeds of Canavalia ensiformis., Hennig M, Jansonius JN, Terwisscha van Scheltinga AC, Dijkstra BW, Schlesier B, J Mol Biol. 1995 Nov 24;254(2):237-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7490746 7490746]
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[[Category: Canavalia ensiformis]]
[[Category: Canavalia ensiformis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hennig, M.]]
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[[Category: Hennig M]]
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[[Category: chitin binding protein]]
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[[Category: plant chitinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:36:40 2007''
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Current revision

CRYSTAL STRUCTURE OF CONCANAVALIN B AT 1.65 A RESOLUTION

PDB ID 1cnv

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