1tlk | pdb_00001tlk

X-RAY STRUCTURE DETERMINATION OF TELOKIN, THE C-TERMINAL DOMAIN OF MYOSIN LIGHT CHAIN KINASE, AT 2.8 ANGSTROMS RESOLUTION

spinqualitylabelsall models 1tlk, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1tlk is a 1 chain structure with sequence from Melga. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: [Myosin_light-chain_kinase [Myosin light-chain] kinase], with EC number 2.7.11.18 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MYLK_MELGA] Corresponds to the C-terminus of smooth muscle myosin light chain kinase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The three-dimensional structure of telokin, an acidic protein identical to the C-terminal portion of smooth muscle myosin light chain kinase from turkey gizzard, has been determined at 2.8 A resolution and refined to a crystallographic R-factor of 19.5% for all measured X-ray data from 30 A to 2.8 A. Crystals used in the investigation belonged to the space group P3(2)21, with one molecule per asymmetric unit and unit cell dimensions of a = b = 64.4 A and c = 50.6 A. Telokin contains 154 amino acid residues, 103 of which were visible in the electron density map. The overall molecular fold of telokin consists of seven strands of antiparallel beta-pleated sheet that wrap around to form a barrel. There is also an extended tail of eight amino acid residues at the N terminus that does not participate in beta-sheet formation. The beta-barrel can be simply envisioned as two layers of beta-sheet, nearly parallel to one another, with one layer containing four and the other three beta-strands. This type of beta-barrel, as seen in telokin, was first observed for the CH2 domain of an immunoglobulin fragment Fc. Telokin is an intracellular protein and, as such, does not contain the disulphide linkage between beta-strands B and F normally observed in the immunoglobulin constant domains. It does, however, contain two cysteine amino acid residues (Cys63 and Cys115) that are situated at structurally identical positions to those forming the disulphide linkage in the immunoglobulin constant domain. X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 A resolution.,Holden HM, Ito M, Hartshorne DJ, Rayment I J Mol Biol. 1992 Oct 5;227(3):840-51. PMID:1404391 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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