PDBsum entry 1m9i

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protein metals links
Lipid binding protein PDB id
Jmol PyMol
Protein chain
664 a.a. *
_CA ×5
Waters ×148
* Residue conservation analysis
PDB id:
Name: Lipid binding protein
Title: Crystal structure of phosphorylation-mimicking mutant t356d of annexin vi
Structure: Annexin vi. Chain: a. Synonym: lipocortin vi, p68, p70, protein iii, chromobindin 20, 67 kda calelectrin, calphobindin-ii, cpb- ii. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: anx6. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
2.65Å     R-factor:   0.225     R-free:   0.279
Authors: C.Freye-Minks,R.H.Kretsinger,C.E.Creutz
Key ref:
C.Freye-Minks et al. (2003). Structural and dynamic changes in human annexin VI induced by a phosphorylation-mimicking mutation, T356D. Biochemistry, 42, 620-630. PubMed id: 12534274 DOI: 10.1021/bi026742h
29-Jul-02     Release date:   07-Aug-02    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P08133  (ANXA6_HUMAN) -  Annexin A6
673 a.a.
664 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   9 terms 
  Biological process     apoptotic signaling pathway   6 terms 
  Biochemical function     protein binding     9 terms  


DOI no: 10.1021/bi026742h Biochemistry 42:620-630 (2003)
PubMed id: 12534274  
Structural and dynamic changes in human annexin VI induced by a phosphorylation-mimicking mutation, T356D.
C.Freye-Minks, R.H.Kretsinger, C.E.Creutz.
Phosphorylation of some members of the annexin family of proteins may play a significant role in controlling their calcium-dependent interactions with membranes. Recent electron microscopic studies of annexin VI revealed that the protein's two core domains exhibit a great degree of flexibility and are able to undergo a relative conformational change that could potentially initiate contacts between membranes [Avila-Sakar, A. J., et al. (2000) J. Struct. Biol. 130, 54-62]. To assess the possibility of a regulatory role of phosphorylation in this behavior, the crystal structure of a phosphorylation-mimicking mutant (T356D in the flexible connector region of human annexin VI) was determined to 2.65 A resolution. When the mutant is compared to the wild-type annexin VI, subtle differences are seen at the site of the mutation, while larger changes are evident in one of the calcium-binding loops and in the presence of five calcium ions. Furthermore, biochemical studies provide evidence for additional conformational differences between the T356D and wild-type solution structures. Fluorescence emission and acrylamide quenching suggest a higher level of solvent exposure of Trp-343 in the connector region of T356D in the presence of calcium. Comparisons of retardation coefficients in native gel electrophoresis reveal that T356D has a more extended shape, while proteolytic studies show a greater accessibility of a trypsin cleavage site inside the linker region, indicating a conformation more open than the wild-type form. These data provide insights into a possible regulatory mechanism leading to a higher degree of flexibility and possibly a higher calcium binding affinity of annexin VI upon phosphorylation.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20888375 C.Enrich, C.Rentero, Muga, M.Reverter, V.Mulay, P.Wood, M.Koese, and T.Grewal (2011).
Annexin A6-Linking Ca(2+) signaling with cholesterol transport.
  Biochim Biophys Acta, 1813, 935-947.  
18044716 A.Strzelecka-Kiliszek, M.E.Buszewska, P.Podszywalow-Bartnicka, S.Pikula, K.Otulak, R.Buchet, and J.Bandorowicz-Pikula (2008).
Calcium- and pH-dependent localization of annexin A6 isoforms in Balb/3T3 fibroblasts reflecting their potential participation in vesicular transport.
  J Cell Biochem, 104, 418-434.  
17613532 B.R.Genge, L.N.Wu, and R.E.Wuthier (2007).
In vitro modeling of matrix vesicle nucleation: synergistic stimulation of mineral formation by annexin A5 and phosphatidylserine.
  J Biol Chem, 282, 26035-26045.  
16359340 A.Fredriksson, M.Ballesteros, S.Dukan, and T.Nyström (2006).
Induction of the heat shock regulon in response to increased mistranslation requires oxidative modification of the malformed proteins.
  Mol Microbiol, 59, 350-359.  
15634682 C.B.Marta, M.B.Montano, C.M.Taylor, A.L.Taylor, R.Bansal, and S.E.Pfeiffer (2005).
Signaling cascades activated upon antibody cross-linking of myelin oligodendrocyte glycoprotein: potential implications for multiple sclerosis.
  J Biol Chem, 280, 8985-8993.  
15928709 V.Gerke, C.E.Creutz, and S.E.Moss (2005).
Annexins: linking Ca2+ signalling to membrane dynamics.
  Nat Rev Mol Cell Biol, 6, 449-461.  
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