4Q6N

Structural analysis of the tripeptide-bound form of Helicobacter pylori Csd4, a D,L-carboxypeptidase

Summary for 4Q6N

• Entry DOI: 10.2210/pdb4q6n/pdb
• Related: 4Q6M 4Q6O 4Q6P 4Q6Q
• Descriptor: Conserved hypothetical secreted protein, L-ALA-GAMMA-D-GLU-MESO-DIAMINOPIMELIC ACID, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: m14 metallopeptidase, d, l-carboxypeptidase, peptidoglycan, csd5, hydrolase
• Biological source: Helicobacter pylori
• Total number of polymer chains: 1
• Total formula weight: 50701.18

Authors

Kim, H.S.,Kim, J.,Im, H.N.,An, D.R.,Lee, M.,Hesek, D.,Mobashery, S.,Kim, J.Y.,Cho, K.,Yoon, H.J.,Han, B.W.,Lee, B.I.,Suh, S.W. (deposition date: 2014-04-23, release date: 2014-11-05, Last modification date: 2024-03-20)

• Primary citation: Kim, H.S.,Kim, J.,Im, H.N.,An, D.R.,Lee, M.,Hesek, D.,Mobashery, S.,Kim, J.Y.,Cho, K.,Yoon, H.J.,Han, B.W.,Lee, B.I.,Suh, S.W.; Structural basis for the recognition of muramyltripeptide by Helicobacter pylori Csd4, a D,L-carboxypeptidase controlling the helical cell shape; Acta Crystallogr.,Sect.D, 70:2800-2812, 2014; PubMed: 25372672; DOI: 10.1107/S1399004714018732

Experimental method

X-RAY DIFFRACTION (1.55 Å)