1cax: Difference between revisions

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New page: left|200px<br /><applet load="1cax" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cax, resolution 2.6Å" /> '''DETERMINATION OF THRE...
 
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[[Image:1cax.jpg|left|200px]]<br /><applet load="1cax" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1cax, resolution 2.6&Aring;" />
'''DETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENT'''<br />


==Overview==
==DETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENT==
Canavalin, the major reserve protein of the jack bean, was obtained in, four different crystal forms. From the structure determined by multiple, isomorphous replacement in a hexagonal unit cell, the structures of three, other crystals were determined by molecular replacement. In two cases, the, rhombohedral and cubic crystals, placement was facilitated by coincidence, of threefold molecular symmetry with crystallographic operators. In the, orthorhombic crystal the canavalin trimer was the asymmetric unit. The, rhombohedral, orthorhombic and cubic crystal structures were subsequently, refined using a combination of several approaches with resulting R factors, of 0.194, 0.185 and 0.211 at resolutions of 2.6, 2.6 and 2.3 A, respectively. Variation in the conformation of the molecule from crystal, to crystal was small with an r.m.s. deviation in Calpha positions of 0.89, A. Packing is quite different among crystal forms but lattice interactions, appear to play little role in the conformation of the molecule. Greatest, variations in mean position are for those residues that also exhibit the, greatest thermal motion. Crystal contacts in all crystals are mediated, almost exclusively by hydrophilic side chains, and three to six, intermolecular salt bridges per protein subunit are present in each case.
<StructureSection load='1cax' size='340' side='right'caption='[[1cax]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1cax]] is a 6 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=1CAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CAX FirstGlance]. <br>
1CAX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1CAX OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#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=1cax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cax OCA], [https://pdbe.org/1cax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cax RCSB], [https://www.ebi.ac.uk/pdbsum/1cax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cax ProSAT]</span></td></tr>
==Reference==
</table>
Determination of three crystal structures of canavalin by molecular replacement., Ko TP, Ng JD, Greenwood A, McPherson A, Acta Crystallogr D Biol Crystallogr. 1993 Sep 1;49(Pt 5):478-89. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299507 15299507]
== Function ==
[https://www.uniprot.org/uniprot/CANA_CANEN CANA_CANEN] Seed storage protein.
== 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/ca/1cax_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=1cax ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Canavalia ensiformis]]
[[Category: Canavalia ensiformis]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Day, J.]]
[[Category: Day J]]
[[Category: Greenwood, A.]]
[[Category: Greenwood A]]
[[Category: Ko, T-P.]]
[[Category: Ko T-P]]
[[Category: McPherson, A.]]
[[Category: McPherson A]]
[[Category: Ng, J.D.]]
[[Category: Ng JD]]
[[Category: seed storage protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:18:37 2007''

Latest revision as of 09:42, 7 February 2024

DETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENTDETERMINATION OF THREE CRYSTAL STRUCTURES OF CANAVALIN BY MOLECULAR REPLACEMENT

Structural highlights

1cax is a 6 chain structure with sequence from Canavalia ensiformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CANA_CANEN Seed storage protein.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1cax, resolution 2.60Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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