3lp9: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(10 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 3lp9 is ON HOLD  until Paper Publication
==Crystal structure of LS24, A Seed Albumin from Lathyrus sativus==
<StructureSection load='3lp9' size='340' side='right'caption='[[3lp9]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3lp9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lathyrus_sativus Lathyrus sativus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LP9 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SPM:SPERMINE'>SPM</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=3lp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lp9 OCA], [https://pdbe.org/3lp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lp9 RCSB], [https://www.ebi.ac.uk/pdbsum/3lp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lp9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ALB2_LATSA ALB2_LATSA] May play a role in response to oxidative stress and polyamine biosynthesis. The monomeric form binds one hemin per monomer. In the dimeric form, about half of the dimers bind one molecule of spermine each under physiological conditions. Ligand binding is mutually exclusive as binding of hemin leads to dissociation of the dimer.<ref>PMID:20147493</ref>
== 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/lp/3lp9_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=3lp9 ConSurf].
<div style="clear:both"></div>


Authors: Gaur, V., Qureshi, I.A., Singh, A., Chanana, V., Salunke, D.M.
==See Also==
 
*[[Albumin 3D structures|Albumin 3D structures]]
Description: Crystal structure of LS24, A Seed Albumin from Lathyrus sativus
== References ==
 
<references/>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 17 10:11:15 2010''
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Lathyrus sativus]]
[[Category: Chanana V]]
[[Category: Gaur V]]
[[Category: Qureshi IA]]
[[Category: Salunke DM]]
[[Category: Singh A]]

Latest revision as of 11:31, 20 March 2024

Crystal structure of LS24, A Seed Albumin from Lathyrus sativusCrystal structure of LS24, A Seed Albumin from Lathyrus sativus

Structural highlights

3lp9 is a 4 chain structure with sequence from Lathyrus sativus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ALB2_LATSA May play a role in response to oxidative stress and polyamine biosynthesis. The monomeric form binds one hemin per monomer. In the dimeric form, about half of the dimers bind one molecule of spermine each under physiological conditions. Ligand binding is mutually exclusive as binding of hemin leads to dissociation of the dimer.[1]

Evolutionary Conservation

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

See Also

References

  1. Gaur V, Qureshi IA, Singh A, Chanana V, Salunke DM. Crystal structure and functional insights of hemopexin fold protein from grass pea. Plant Physiol. 2010 Apr;152(4):1842-50. Epub 2010 Feb 10. PMID:20147493 doi:10.1104/pp.109.150680

3lp9, resolution 2.20Å

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