1dm5 is a 6 chain structure with sequence from Hydvu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Annexins are a family of calcium- and phospholipid-binding proteins involved with numerous cellular processes including membrane fusion, ion channel activity, and heterocomplex formation with other proteins. The annexin XII (ANXB12) crystal structure presented evidence that calcium mediates the formation of a hexamer through a novel intermolecular calcium-binding site [Luecke et al. (1995) Nature 378, 512-515]. In an attempt to disrupt hexamerization, we mutated a conserved key ligand in the intermolecular calcium-binding site, Glu105, to lysine. Despite its occurrence in a new spacegroup, the 1.93 A resolution structure reveals a hexamer with the Lys105 epsilon-amino group nearly superimposable with the original intermolecular calcium position. Our analysis shows that the mutation is directly involved in stabilizing the hexamer. The local residues are reoriented to retain affinity between the two trimers via a pH-dependent switch residue, Glu76, which is now protonated, allowing it to form tandem hydrogen bonds with the backbone carbonyl and nitrogen atoms of Thr103 located across the trimer interface. The loss of the intermolecular calcium-binding site is recuperated by extensive hydrogen bonding favoring hexamer stabilization. The presence of this mutant structure provides further evidence for hexameric annexin XII, and possible in vivo roles are discussed.
Annexin XII E105K crystal structure: identification of a pH-dependent switch for mutant hexamerization.,Cartailler JP, Haigler HT, Luecke H Biochemistry. 2000 Mar 14;39(10):2475-83. PMID:10704197[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑Cartailler JP, Haigler HT, Luecke H. Annexin XII E105K crystal structure: identification of a pH-dependent switch for mutant hexamerization. Biochemistry. 2000 Mar 14;39(10):2475-83. PMID:10704197
