3UMQ

Crystal structure of peptidoglycan recognition protein-S complexed with butyric acid at 2.2 A resolution

Summary for 3UMQ

• Entry DOI: 10.2210/pdb3umq/pdb
• Related: 3C2X
• Descriptor: Peptidoglycan recognition protein 1, butanoic acid, GLYCEROL, ... (4 entities in total)
• Functional Keywords: immune response, secreted, antimicrobial, pgrp, recognition protein, antibacterial, peptidoglycan binding, butyric acid, immune system
• Biological source: Camelus dromedarius (camel)
• Cellular location: Secreted (By similarity): Q9GK12
• Total number of polymer chains: 4
• Total formula weight: 76226.03

Authors

Pandey, N.,Sharma, P.,Sinha, M.,Bhushan, A.,Kaur, P.,Sharma, S.,Singh, T.P. (deposition date: 2011-11-14, release date: 2012-07-04, Last modification date: 2023-11-01)

Primary citation

Sharma, P.,Yamini, S.,Dube, D.,Singh, A.,Mal, G.,Pandey, N.,Sinha, M.,Singh, A.K.,Dey, S.,Kaur, P.,Mitra, D.K.,Sharma, S.,Singh, T.P.
Structural basis of the binding of fatty acids to peptidoglycan recognition protein, PGRP-S through second binding site
Arch.Biochem.Biophys., 529:1-10, 2013

PubMed Abstract: Short peptidoglycan recognition protein (PGRP-S) is a member of the mammalian innate immune system. PGRP-S from Camelus dromedarius (CPGRP-S) has been shown to bind to lipopolysaccharide (LPS), lipoteichoic acid (LTA) and peptidoglycan (PGN). Its structure consists of four molecules A, B, C and D with ligand binding clefts situated at A-B and C-D contacts. It has been shown that LPS, LTA and PGN bind to CPGRP-S at C-D contact. The cleft at the A-B contact indicated features that suggested a possible binding of fatty acids including mycolic acid of Mycobacterium tuberculosis. Therefore, binding studies of CPGRP-S were carried out with fatty acids, butyric acid, lauric acid, myristic acid, stearic acid and mycolic acid which showed affinities in the range of 10(-5) to 10(-8) M. Structure determinations of the complexes of CPGRP-S with above fatty acids showed that they bound to CPGRP-S in the cleft at the A-B contact. The flow cytometric studies showed that mycolic acid induced the production of pro-inflammatory cytokines, TNF-α and IFN-γ by CD3+ T cells. The concentrations of cytokines increased considerably with increasing concentrations of mycolic acid. However, their levels decreased substantially on adding CPGRP-S.

PubMed: 23149273
DOI: 10.1016/j.abb.2012.11.001

Experimental method

X-RAY DIFFRACTION (2.2 Å)