2XWG

Crystal structure of sortase C-1 from Actinomyces oris (formerly Actinomyces naeslundii)

Summary for 2XWG

Entry DOI	10.2210/pdb2xwg/pdb
Descriptor	SORTASE, CALCIUM ION (3 entities in total)
Functional Keywords	hydrolase, fimbrial assembly
Biological source	ACTINOMYCES ORIS
Total number of polymer chains	5
Total formula weight	130816.55
Authors	Persson, K. (deposition date: 2010-11-02, release date: 2011-02-23, Last modification date: 2023-12-20)
Primary citation	Persson, K. Structure of the Sortase Acsrtc-1 from Actinomyces Oris Acta Crystallogr.,Sect.D, 67:212-, 2011 Cited by PubMed Abstract: The crystal structure of the sortase AcSrtC-1 from the oral microorganism Actinomyces oris has been determined to 2.4 Å resolution. AcSrtC-1 is a cysteine transpeptidase that is responsible for the formation of fimbriae by the polymerization of a shaft protein. Similar to other pili-associated sortases, the AcSrtC-1 active site is protected by a flexible lid. The asymmetric unit contains five AcSrtC-1 molecules and their catalytic Cys-His-Arg triads are trapped in two different conformations. It is also shown that the thermostability of the enzyme is increased by the presence of calcium. PubMed: 21358052 DOI: 10.1107/S0907444911004215 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.4 Å)

Structure validation