1cnr: Difference between revisions
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< | ==CORRELATED DISORDER OF THE PURE PRO22(SLASH)LEU25 FORM OF CRAMBIN AT 150K REFINED TO 1.05 ANGSTROMS RESOLUTION== | ||
The | <StructureSection load='1cnr' size='340' side='right'caption='[[1cnr]], [[Resolution|resolution]] 1.05Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1cnr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Crambe_hispanica_subsp._abyssinica Crambe hispanica subsp. abyssinica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CNR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CNR 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]] 1.05Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene></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=1cnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cnr OCA], [https://pdbe.org/1cnr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cnr RCSB], [https://www.ebi.ac.uk/pdbsum/1cnr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cnr ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CRAM_CRAAB CRAM_CRAAB] The function of this hydrophobic plant seed protein is not known. | |||
== 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/cn/1cnr_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1cnr ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The high resolution crystal structure of crambin has been based on the crystals containing two sequence forms (the mixed form). Here, we report the crystal structure of the sequence isomer having Pro and Leu at residues 22 and 25 (the PL form). This elimination of the sequence heterogeneity resulted in a simpler structure which permits a more accurate modeling of protein disorder. In the observed disorder, the PL form structure and the mixed form structure have significant differences: 1) the disorder caused by the sequence heterogeneity (Pro2/Ser22, Leu/Ile25, Tyr29) is absent in the PL form; 2) Phe13 and Glu23 disordered in the mixed form have only one conformation in the PL form; and 3) Asn12 has multiple conformations in the PL form. During the study of disorder in the PL form structure, we found that conformational correlation can be inferred from a structure determined with Bragg's reflections by introducing fundamental stereochemical information, van der Waals contact (Gursky, O., Badger, J., Li, Y., and Caspar, D. L. D. (1992) Biophys. J. 63, 1210-1220), although an x-ray structure is an image averaged over a large number of copies and the period of data collection and does not carry direct evidence about correlations. The correlations among Thr2,Arg10, and Ile34 present the clearest example. The dimension of this correlation is comparable with the short-range (4-8 A) correlations in the atomic displacements concluded from the x-ray diffuse scattering experiments (Caspar, D. L. D., Clarage, J. B., Salunke, D. M., and Clarage, M. S. (1988) Nature 322, 659-662; Clarage, J. B., Clarage, M. S., Phillips, W. C., Sweet, R. M., and Caspar, D. L. D. (1992) Proteins 12, 145-157). | |||
Correlated disorder of the pure Pro22/Leu25 form of crambin at 150 K refined to 1.05-A resolution.,Yamano A, Teeter MM J Biol Chem. 1994 May 13;269(19):13956-65. PMID:8188676<ref>PMID:8188676</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1cnr" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
[[Category: Crambe hispanica subsp. abyssinica]] | [[Category: Crambe hispanica subsp. abyssinica]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Teeter | [[Category: Teeter MM]] | ||
[[Category: Yamano | [[Category: Yamano A]] | ||
Latest revision as of 11:22, 6 November 2024
CORRELATED DISORDER OF THE PURE PRO22(SLASH)LEU25 FORM OF CRAMBIN AT 150K REFINED TO 1.05 ANGSTROMS RESOLUTIONCORRELATED DISORDER OF THE PURE PRO22(SLASH)LEU25 FORM OF CRAMBIN AT 150K REFINED TO 1.05 ANGSTROMS RESOLUTION
Structural highlights
FunctionCRAM_CRAAB The function of this hydrophobic plant seed protein is not known. 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 PubMedThe high resolution crystal structure of crambin has been based on the crystals containing two sequence forms (the mixed form). Here, we report the crystal structure of the sequence isomer having Pro and Leu at residues 22 and 25 (the PL form). This elimination of the sequence heterogeneity resulted in a simpler structure which permits a more accurate modeling of protein disorder. In the observed disorder, the PL form structure and the mixed form structure have significant differences: 1) the disorder caused by the sequence heterogeneity (Pro2/Ser22, Leu/Ile25, Tyr29) is absent in the PL form; 2) Phe13 and Glu23 disordered in the mixed form have only one conformation in the PL form; and 3) Asn12 has multiple conformations in the PL form. During the study of disorder in the PL form structure, we found that conformational correlation can be inferred from a structure determined with Bragg's reflections by introducing fundamental stereochemical information, van der Waals contact (Gursky, O., Badger, J., Li, Y., and Caspar, D. L. D. (1992) Biophys. J. 63, 1210-1220), although an x-ray structure is an image averaged over a large number of copies and the period of data collection and does not carry direct evidence about correlations. The correlations among Thr2,Arg10, and Ile34 present the clearest example. The dimension of this correlation is comparable with the short-range (4-8 A) correlations in the atomic displacements concluded from the x-ray diffuse scattering experiments (Caspar, D. L. D., Clarage, J. B., Salunke, D. M., and Clarage, M. S. (1988) Nature 322, 659-662; Clarage, J. B., Clarage, M. S., Phillips, W. C., Sweet, R. M., and Caspar, D. L. D. (1992) Proteins 12, 145-157). Correlated disorder of the pure Pro22/Leu25 form of crambin at 150 K refined to 1.05-A resolution.,Yamano A, Teeter MM J Biol Chem. 1994 May 13;269(19):13956-65. PMID:8188676[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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