1f55: Difference between revisions

Revision as of 02:42, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1f55.png

Template:STRUCTURE 1f55

SOLUTION STRUCTURE OF THE CALCIUM BOUND N-TERMINAL DOMAIN OF YEAST CALMODULINSOLUTION STRUCTURE OF THE CALCIUM BOUND N-TERMINAL DOMAIN OF YEAST CALMODULIN

Template:ABSTRACT PUBMED 11076504

About this StructureAbout this Structure

1F55 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA.

ReferenceReference

Solution structures of the N-terminal domain of yeast calmodulin: Ca2+-dependent conformational change and its functional implication., Ishida H, Takahashi K, Nakashima K, Kumaki Y, Nakata M, Hikichi K, Yazawa M, Biochemistry. 2000 Nov 14;39(45):13660-8. PMID:11076504

Page seeded by OCA on Tue Jul 1 02:42:44 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1f55.jpg|left|200px]]
+{{Seed}}
+[[Image:1f55.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1f55|  PDB=1f55  |  SCENE=  }}
-'''SOLUTION STRUCTURE OF THE CALCIUM BOUND N-TERMINAL DOMAIN OF YEAST CALMODULIN'''
+===SOLUTION STRUCTURE OF THE CALCIUM BOUND N-TERMINAL DOMAIN OF YEAST CALMODULIN===
-==Overview==
+<!--
-We have determined solution structures of the N-terminal half domain (N-domain) of yeast calmodulin (YCM0-N, residues 1-77) in the apo and Ca(2+)-saturated forms by NMR spectroscopy. The Ca(2+)-binding sites of YCM0-N consist of a pair of helix-loop-helix motifs (EF-hands), in which the loops are linked by a short beta-sheet. The binding of two Ca(2+) causes large rearrangement of the four alpha-helices and exposes the hydrophobic surface as observed for vertebrate calmodulin (CaM). Within the observed overall conformational similarity in the peptide backbone, several significant conformational differences were observed between the two proteins, which originated from the 38% disagreement in amino acid sequences. The beta-sheet in apo YCM0-N is strongly twisted compared with that in the N-domain of CaM, while it turns to the normal more stable conformation on Ca(2+) binding. YCM0-N shows higher cooperativity in Ca(2+) binding than the N-domain of CaM, and the observed conformational change of the beta-sheet is a possible cause of the highly cooperative Ca(2+) binding. The hydrophobic surface on Ca(2+)-saturated YCM0-N appears less flexible due to the replacements of Met51, Met71, and Val55 in the hydrophobic surface of CaM with Leu51, Leu71, and Ile55, which is thought to be one of reasons for the poor activation of target enzymes by yeast CaM.
+The line below this paragraph, {{ABSTRACT_PUBMED_11076504}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11076504 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11076504}}
 ==About this Structure==
-F55 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F55 OCA].
+F55 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F55 OCA].
 ==Reference==
@@ Line 31: / Line 35: @@
 [[Category: Ef-hand]]
 [[Category: Helix-loop-helix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:54:53 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 02:42:44 2008''