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[[Image:2o9o.png|left|200px]]
==Crystal Structure of the buffalo Secretory Signalling Glycoprotein at 2.8 A resolution==
<StructureSection load='2o9o' size='340' side='right' caption='[[2o9o]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2o9o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bubalus_bubalis Bubalus bubalis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1sv8 1sv8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O9O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O9O FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2esc|2esc]], [[2dpe|2dpe]]</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2o9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o9o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2o9o RCSB], [http://www.ebi.ac.uk/pdbsum/2o9o PDBsum]</span></td></tr>
<table>
== 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/o9/2o9o_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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of a 40 kDa signalling glycoprotein from buffalo (SPB-40) has been determined at 2.8 A resolution. SPB-40 acts as a protective signalling factor by binding to viable cells during the early phase of involution, during which extensive tissue remodelling occurs. It was isolated from the dry secretions of Murrah buffalo. It was purified and crystallized using the hanging-drop vapour-diffusion method with 19% ethanol as the precipitant. The protein was also cloned and its complete nucleotide and amino-acid sequences were determined. When compared with the sequences of other members of the family, the sequence of SPB-40 revealed two very important mutations in the sugar-binding region, in which Tyr120 changed to Trp120 and Glu269 changed to Trp269. The structure showed a significant distortion in the shape of the sugar-binding groove. The water structure in the groove is also drastically altered. The folding of the protein chain in the flexible region comprising segments His188-His197, Phe202-Arg212 and Tyr244-Pro260 shows large variations when compared with other proteins of the family.


{{STRUCTURE_2o9o|  PDB=2o9o  |  SCENE=  }}
Structure of the buffalo secretory signalling glycoprotein at 2.8 A resolution.,Ethayathulla AS, Srivastava DB, Kumar J, Saravanan K, Bilgrami S, Sharma S, Kaur P, Srinivasan A, Singh TP Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt, 4):258-65. Epub 2007 Mar 12. PMID:17401190<ref>PMID:17401190</ref>


===Crystal Structure of the buffalo Secretory Signalling Glycoprotein at 2.8 A resolution===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_17401190}}
 
==About this Structure==
[[2o9o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bubalus_bubalis Bubalus bubalis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1sv8 1sv8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O9O OCA].


==See Also==
==See Also==
*[[Chitinase-3-like protein 1|Chitinase-3-like protein 1]]
*[[Chitinase-3-like protein 1|Chitinase-3-like protein 1]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:017401190</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Bubalus bubalis]]
[[Category: Bubalus bubalis]]
[[Category: Ethayathulla, A S.]]
[[Category: Ethayathulla, A S.]]

Revision as of 07:57, 29 September 2014

Crystal Structure of the buffalo Secretory Signalling Glycoprotein at 2.8 A resolutionCrystal Structure of the buffalo Secretory Signalling Glycoprotein at 2.8 A resolution

Structural highlights

2o9o is a 1 chain structure with sequence from Bubalus bubalis. This structure supersedes the now removed PDB entry 1sv8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Related:2esc, 2dpe
Resources:FirstGlance, OCA, RCSB, PDBsum

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 crystal structure of a 40 kDa signalling glycoprotein from buffalo (SPB-40) has been determined at 2.8 A resolution. SPB-40 acts as a protective signalling factor by binding to viable cells during the early phase of involution, during which extensive tissue remodelling occurs. It was isolated from the dry secretions of Murrah buffalo. It was purified and crystallized using the hanging-drop vapour-diffusion method with 19% ethanol as the precipitant. The protein was also cloned and its complete nucleotide and amino-acid sequences were determined. When compared with the sequences of other members of the family, the sequence of SPB-40 revealed two very important mutations in the sugar-binding region, in which Tyr120 changed to Trp120 and Glu269 changed to Trp269. The structure showed a significant distortion in the shape of the sugar-binding groove. The water structure in the groove is also drastically altered. The folding of the protein chain in the flexible region comprising segments His188-His197, Phe202-Arg212 and Tyr244-Pro260 shows large variations when compared with other proteins of the family.

Structure of the buffalo secretory signalling glycoprotein at 2.8 A resolution.,Ethayathulla AS, Srivastava DB, Kumar J, Saravanan K, Bilgrami S, Sharma S, Kaur P, Srinivasan A, Singh TP Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt, 4):258-65. Epub 2007 Mar 12. PMID:17401190[1]

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

See Also

References

  1. ↑ Ethayathulla AS, Srivastava DB, Kumar J, Saravanan K, Bilgrami S, Sharma S, Kaur P, Srinivasan A, Singh TP. Structure of the buffalo secretory signalling glycoprotein at 2.8 A resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt, 4):258-65. Epub 2007 Mar 12. PMID:17401190 doi:http://dx.doi.org/10.1107/S1744309107010445

2o9o, resolution 2.80Å

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