4cln

<table><tr><td colspan='2'>[[4cln]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CLN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CLN 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>

<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=4cln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cln OCA], [http://pdbe.org/4cln PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cln RCSB], [http://www.ebi.ac.uk/pdbsum/4cln PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cln ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CALM_DROME CALM_DROME]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The crystal structure of calmodulin (Mr 16,700, 148 residues) from Drosophila melanogaster as expressed in a bacterial system has been determined and refined at 2.2-A resolution. Starting with the structure of mammalian calmodulin, we produced an extensively refitted and refined model with a conventional crystallographic R value of 0.197 for the 5,239 reflections (F greater than or equal to 2 sigma (F)) within the 10.0-2.2-A resolution range. The model includes 1,164 protein atoms, 4 calcium ions, and 78 water molecules and has root mean square deviations from standard values of 0.018 A for bond lengths and 0.043 A for angle distances. The overall structure is similar to mammalian calmodulin, with a seven-turn central helix connecting the two calcium-binding domains. The "dumb-bell" shaped molecule contains seven alpha-helices and four "EF hand" calcium-binding sites. Although the amino acid sequences of mammalian and Drosophila calmodulins differ by only three conservative amino acid changes, the refined model reveals a number of significant differences between the two structures. Superimposition of the structures yields a root mean square deviation of 1.22 A for the 1,120 equivalent atoms. The calcium-binding domains have a root mean square deviation of 0.85 A for the 353 equivalent atoms. There are also differences in the amino terminus, the bend of the central alpha-helix, and the orientations of some of the side chains.

Structure of a recombinant calmodulin from Drosophila melanogaster refined at 2.2-A resolution.,Taylor DA, Sack JS, Maune JF, Beckingham K, Quiocho FA J Biol Chem. 1991 Nov 15;266(32):21375-80. PMID:1939171<ref>PMID:1939171</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 4cln" style="background-color:#fffaf0;"></div>

*[[Calmodulin|Calmodulin]]

[[Category: Drome]]

[[Category: Beckingham, K]]

[[Category: Maune, J F]]

[[Category: Quiocho, F A]]

[[Category: Sack, J S]]

[[Category: Taylor, D A]]

[[Category: Calcium binding protein]]