5KVP
Solution structure of the catalytic domain of zoocin A
Summary for 5KVP
Entry DOI | 10.2210/pdb5kvp/pdb |
NMR Information | BMRB: 30139 |
Descriptor | Zoocin A endopeptidase, ZINC ION, UNKNOWN LIGAND (3 entities in total) |
Functional Keywords | hydrolase, exoenzyme, anti-microbial, endopeptidase |
Biological source | Streptococcus equi subsp. zooepidemicus |
Total number of polymer chains | 1 |
Total formula weight | 16919.09 |
Authors | Timkovich, R.,Xing, M.,Simmonds, R.S. (deposition date: 2016-07-15, release date: 2016-10-26, Last modification date: 2024-05-01) |
Primary citation | Xing, M.,Simmonds, R.S.,Timkovich, R. Solution structure of the Cys74 to Ala74 mutant of the recombinant catalytic domain of Zoocin A. Proteins, 85:177-181, 2017 Cited by PubMed Abstract: Zoocin A is a Zn-metallopeptidase secreted by Streptococcus zooepidemicus strain 4881. Its catalytic domain is responsible for cleaving the D-alanyl-L-alanine peptide bond in streptococcal peptidoglycan. The solution NMR structure of the Cys74 to Ala74 mutant of the recombinant catalytic domain (rCAT C74A) has been determined. With a previous structure determination for the recombinant target recognition domain (rTRD), this completes the 3D structure of zoocin A. While the structure of rCAT C74A resembles those of the catalytic domains of lysostaphin and LytM, the substrate binding groove is wider and no tyrosine residue was observed in the active site. Proteins 2016; 85:177-181. © 2016 Wiley Periodicals, Inc. PubMed: 27699884DOI: 10.1002/prot.25178 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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