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[[Image:1pvb.jpg|left|200px]]<br /><applet load="1pvb" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1pvb, resolution 1.75&Aring;" />
'''X-RAY STRUCTURE OF A NEW CRYSTAL FORM OF PIKE 4.10 PARVALBUMIN'''<br />


==Overview==
==X-RAY STRUCTURE OF A NEW CRYSTAL FORM OF PIKE 4.10 PARVALBUMIN==
<StructureSection load='1pvb' size='340' side='right'caption='[[1pvb]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1pvb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Esox_lucius Esox lucius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PVB 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]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</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=1pvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pvb OCA], [https://pdbe.org/1pvb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pvb RCSB], [https://www.ebi.ac.uk/pdbsum/1pvb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pvb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRVB_ESOLU PRVB_ESOLU] In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions.
== 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/pv/1pvb_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=1pvb ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A new crystal form of pike (pI 4.10) parvalbumin has been crystallized in presence of EDTA at pH 8.0. The crystals are orthorhombic, space group P2(1)2(1)2(1), with a = 51.84, b = 49.95, c = 34.96 A. Diffractometer data were collected to 1.75 A. The structure was solved by molecular replacement and refined to R = 0.168 for 7774 observed reflections [I&gt;/= 2sigma(I)] in the range 8.0-1.75 A. In spite of the presence of EDTA, calcium ions are present in both primary binding sites. As compared to the previously reported structures, the main differences concern the conformation of the N-terminal residues and the packing in the unit cell.
A new crystal form of pike (pI 4.10) parvalbumin has been crystallized in presence of EDTA at pH 8.0. The crystals are orthorhombic, space group P2(1)2(1)2(1), with a = 51.84, b = 49.95, c = 34.96 A. Diffractometer data were collected to 1.75 A. The structure was solved by molecular replacement and refined to R = 0.168 for 7774 observed reflections [I&gt;/= 2sigma(I)] in the range 8.0-1.75 A. In spite of the presence of EDTA, calcium ions are present in both primary binding sites. As compared to the previously reported structures, the main differences concern the conformation of the N-terminal residues and the packing in the unit cell.


==About this Structure==
X-ray structure of a new crystal form of pike 4.10 beta parvalbumin.,Declercq JP, Tinant B, Parello J Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):165-9. PMID:15299738<ref>PMID:15299738</ref>
1PVB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Esox_lucius Esox lucius] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=NH4:'>NH4</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PVB OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
X-ray structure of a new crystal form of pike 4.10 beta parvalbumin., Declercq JP, Tinant B, Parello J, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):165-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299738 15299738]
</div>
<div class="pdbe-citations 1pvb" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Parvalbumin|Parvalbumin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Esox lucius]]
[[Category: Esox lucius]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Declercq, J P.]]
[[Category: Declercq JP]]
[[Category: Parello, J.]]
[[Category: Parello J]]
[[Category: Tinant, B.]]
[[Category: Tinant B]]
[[Category: ACE]]
[[Category: CA]]
[[Category: NH4]]
[[Category: calcium binding protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:53 2008''

Latest revision as of 10:34, 23 October 2024

X-RAY STRUCTURE OF A NEW CRYSTAL FORM OF PIKE 4.10 PARVALBUMINX-RAY STRUCTURE OF A NEW CRYSTAL FORM OF PIKE 4.10 PARVALBUMIN

Structural highlights

1pvb is a 1 chain structure with sequence from Esox lucius. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.75Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PRVB_ESOLU In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions.

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

A new crystal form of pike (pI 4.10) parvalbumin has been crystallized in presence of EDTA at pH 8.0. The crystals are orthorhombic, space group P2(1)2(1)2(1), with a = 51.84, b = 49.95, c = 34.96 A. Diffractometer data were collected to 1.75 A. The structure was solved by molecular replacement and refined to R = 0.168 for 7774 observed reflections [I>/= 2sigma(I)] in the range 8.0-1.75 A. In spite of the presence of EDTA, calcium ions are present in both primary binding sites. As compared to the previously reported structures, the main differences concern the conformation of the N-terminal residues and the packing in the unit cell.

X-ray structure of a new crystal form of pike 4.10 beta parvalbumin.,Declercq JP, Tinant B, Parello J Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):165-9. PMID:15299738[1]

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

See Also

References

  1. ↑ Declercq JP, Tinant B, Parello J. X-ray structure of a new crystal form of pike 4.10 beta parvalbumin. Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):165-9. PMID:15299738 doi:10.1107/S0907444995010006

1pvb, resolution 1.75Å

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