2lc5: Difference between revisions

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<StructureSection load='2lc5' size='340' side='right' caption='[[2lc5]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2lc5' size='340' side='right' caption='[[2lc5]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2lc5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2ktg 2ktg]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LC5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LC5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2lc5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Entamoeba_histolytica_hm-1:imss Entamoeba histolytica hm-1:imss]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2ktg 2ktg]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LC5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LC5 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EHI_100270 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5759 Entamoeba histolytica])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EHI_100270 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294381 Entamoeba histolytica HM-1:IMSS])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lc5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lc5 RCSB], [http://www.ebi.ac.uk/pdbsum/2lc5 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lc5 OCA], [http://pdbe.org/2lc5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lc5 RCSB], [http://www.ebi.ac.uk/pdbsum/2lc5 PDBsum]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 2lc5" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Entamoeba histolytica]]
[[Category: Entamoeba histolytica hm-1:imss]]
[[Category: Barnwal, R P]]
[[Category: Barnwal, R P]]
[[Category: Bhattacharya, A]]
[[Category: Bhattacharya, A]]
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[[Category: Cam-like]]
[[Category: Cam-like]]
[[Category: Ehcam]]
[[Category: Ehcam]]
[[Category: Entamoeba histolytica]]
[[Category: Metal binding protein]]
[[Category: Metal binding protein]]
[[Category: Partially structured protein]]
[[Category: Partially structured protein]]

Revision as of 00:10, 11 September 2015

Calmodulin-like Protein from Entamoeba histolytica: Solution Structure and Calcium-Binding Properties of a Partially Folded ProteinCalmodulin-like Protein from Entamoeba histolytica: Solution Structure and Calcium-Binding Properties of a Partially Folded Protein

Structural highlights

2lc5 is a 1 chain structure with sequence from Entamoeba histolytica hm-1:imss. This structure supersedes the now removed PDB entry 2ktg. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:EHI_100270 (Entamoeba histolytica HM-1:IMSS)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Publication Abstract from PubMed

The mechanism of Ca(2+)-signaling in the protozoan parasite Entamoeba histolytica is yet to be understood as many of the key regulators are still to be identified. E. histolytica encodes a number of multi-EF-hand Ca(2+)-binding proteins (EhCaBPs). Functionally only one of these molecules, EhCaBP1, has been characterized to date. The calmodulin-like protein from E. histolytica (abbreviated as EhCaM or EhCaBP3) is a 17.23 kDa monomeric protein that shows maximum sequence identity with heterologous calmodulins (CaMs). Though CaM activity has been biochemically shown in E. histolytica, there are no reports on the presence of a typical CaM. In an attempt to understand the structural and functional similarity of EhCaM with CaM, we have determined the three-dimensional (3D) solution structure of EhCaM using NMR. The EhCaM has a well-folded N-terminal domain and an unstructured C-terminal counterpart. Further, it sequentially binds only two calcium ions, an unusual mode of Ca(2+)-binding among the known CaBPs, notably both in the N-terminal domain of EhCaM. Further, EhCaM is present in the nucleus in addition to the cytoplasm as detected by immunofluorescence staining, unlike other EhCaBPs that are detected only in the cytoplasm. Therefore, this protein is likely to have a different function. The presence of unusual and a diverse set of CaBPs in E. histolytica suggests a distinct Ca(2+)-signaling process in E. histolytica. The results reported here help in understanding the structure-function relationship of CaBPs including their Ca(2+)-binding properties.

Calmodulin-like Protein from Entamoeba histolytica: Solution Structure and Calcium-Binding Properties of a Partially Folded Protein.,Rout AK, Padhan N, Barnwal RP, Bhattacharya A, Chary KV Biochemistry. 2010 Dec 21. PMID:21114322[1]

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

References

  1. Rout AK, Padhan N, Barnwal RP, Bhattacharya A, Chary KV. Calmodulin-like Protein from Entamoeba histolytica: Solution Structure and Calcium-Binding Properties of a Partially Folded Protein. Biochemistry. 2010 Dec 21. PMID:21114322 doi:10.1021/bi101411q
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