PDBsum entry 1f55

Transport protein

PDB id

1f55

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Contents

			Protein chain

					77 a.a. *

			Metals

					_CA ×2

* Residue conservation analysis

PDB id:

1f55

Links

Name:

Transport protein

Title:

Solution structure of the calcium bound n-terminal domain of yeast calmodulin

Structure:

Calmodulin. Chain: a. Fragment: n-terminal domain. Engineered: yes. Other_details: intracellular calcium sensor

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

30 models

Authors:

H.Ishida,K.Takahashi,K.Nakashima,Y.Kumaki,M.Nakata,K.Hikichi,M.Yazawa

Key ref:

H.Ishida et al. (2000). Solution structures of the N-terminal domain of yeast calmodulin: Ca2+-dependent conformational change and its functional implication. Biochemistry, 39, 13660-13668. PubMed id: 11076504 DOI: 10.1021/bi000582x

Date:

13-Jun-00

Release date:

15-Jul-03

PROCHECK

	Headers

	References

Protein chain

P06787 (CALM_YEAST) - Calmodulin from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: Struc:					147 a.a. 77 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

DOI no: 10.1021/bi000582x	Biochemistry 39:13660-13668 (2000)
PubMed id: 11076504

Solution structures of the N-terminal domain of yeast calmodulin: Ca2+-dependent conformational change and its functional implication.
H.Ishida, K.Takahashi, K.Nakashima, Y.Kumaki, M.Nakata, K.Hikichi, M.Yazawa.

ABSTRACT

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.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20401735

J.L.Kitevski-Leblanc, F.Evanics, and R.Scott Prosser (2010).
Approaches to the assignment of (19)F resonances from 3-fluorophenylalanine labeled calmodulin using solution state NMR.

J Biomol NMR, 47, 113-123.

19217845

E.Laine, A.Blondel, and T.E.Malliavin (2009).
Dynamics and energetics: a consensus analysis of the impact of calcium on EF-CaM protein complex.

Biophys J, 96, 1249-1263.

18175311

E.Laine, J.D.Yoneda, A.Blondel, and T.E.Malliavin (2008).
The conformational plasticity of calmodulin upon calcium complexation gives a model of its interaction with the oedema factor of Bacillus anthracis.

Proteins, 71, 1813-1829.

18075677

N.V.Valeyev, P.Heslop-Harrison, I.Postlethwaite, N.V.Kotov, and D.G.Bates (2008).
Multiple calcium binding sites make calmodulin multifunctional.

Mol Biosyst, 4, 66-73.

17942116

J.T.Warren, Q.Guo, and W.J.Tang (2007).
A 1.3-A structure of zinc-bound N-terminal domain of calmodulin elucidates potential early ion-binding step.

J Mol Biol, 374, 517-527.

PDB code:

2pq3

12557181

L.A.Faga, B.R.Sorensen, W.S.VanScyoc, and M.A.Shea (2003).
Basic interdomain boundary residues in calmodulin decrease calcium affinity of sites I and II by stabilizing helix-helix interactions.

Proteins, 50, 381-391.

11901148

J.Y.Choi, S.H.Lee, C.Y.Park, W.D.Heo, J.C.Kim, M.C.Kim, W.S.Chung, B.C.Moon, Y.H.Cheong, C.Y.Kim, J.H.Yoo, J.C.Koo, H.M.Ok, S.W.Chi, S.E.Ryu, S.Y.Lee, C.O.Lim, and M.J.Cho (2002).
Identification of calmodulin isoform-specific binding peptides from a phage-displayed random 22-mer peptide library.

J Biol Chem, 277, 21630-21638.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.