3i77 | pdb_00003i77

35/99/170-loops of FXa in SGT

spinqualitylabelsall models 3i77, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3i77 is a 1 chain structure with sequence from "actinomyces_griseus"_krainsky_1914 "actinomyces griseus" krainsky 1914. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, CA, SO4 Related: 3i78, 1os8, 2fmj, 3beu Gene: sprT ("Actinomyces griseus" Krainsky 1914) Activity: Trypsin, with EC number 3.4.21.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 Converting one enzyme into another is challenging due to the uneven distribution of important amino acids for function in both protein sequence and structure. We report a strategy for protein engineering allowing an organized mixing and matching of genetic material that leverages lower throughput with increased quality of screens. Our approach successfully tested the contribution of each surface-exposed loop in the trypsin fold alone and the cooperativity of their combinations towards building the substrate selectivity and Na(+)-dependent allosteric activation of the protease domain of human coagulation factor Xa into a bacterial trypsin. As the created proteases lack additional protein domains and protein co-factor activation mechanism requisite for the complexity of blood coagulation, they are stepping-stones towards further understanding and engineering of artificial clotting factors. Combinatorial enzyme design probes allostery and cooperativity in the trypsin fold.,Page MJ, Di Cera E J Mol Biol. 2010 Jun 4;399(2):306-19. Epub 2010 Apr 24. PMID:20399789 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Trypsin

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