Database accession: MF7000871
Name: Rv3272, mutant D175A (Mycobacterium tuberculosis)
PDB ID: 5yiy
Experimental method: X-ray (2.50 Å)
Assembly: Homodimer
Source organism: Mycobacterium tuberculosis
Primary publication of the structure:
Karade SS, Pandey S, Ansari A, Das S, Tripathi S, Arora A, Chopra S, Pratap JV, Dasgupta A
Rv3272 encodes a novel Family III CoA transferase that alters the cell wall lipid profile and protects mycobacteria from acidic and oxidative stress.
(2019) Biochim Biophys Acta Proteins Proteom 1867: 317-330
PMID: 30342240
Abstract:
The availability of complete genome sequence of Mycobacterium tuberculosis has provided an important tool to understand the mycobacterial biology with respect to host-pathogen interaction, which is an unmet need of the hour owing to continuous increasing drug resistance. Hypothetical proteins are often an overlooked pool though half the genome encodes for such proteins of unknown function that could potentially play vital roles in mycobacterial biology. In this context, we report the structural and functional characterization of the hypothetical protein Rv3272. Sequence analysis classifies Rv3272 as a Family III CoA transferase with the classical two domain structure and conserved Aspartate residue (D175). The crystal structure of the wild type protein (2.2 Å) demonstrated the associated inter-locked dimer while that of the D175A mutant co-crystallized with octanoyl-CoA demonstrated relative movement between the two domains. Isothermal titration calorimetry studies indicate that Rv3272 binds to fatty acyl-CoAs of varying carbon chain lengths, with palmitoyl-CoA (C16:0) exhibiting maximum affinity. To determine the functional relevance of Rv3272 in mycobacterial biology, we ectopically expressed Rv3272 in M. smegmatis and assessed that its expression encodes significant alteration in cell surface with marked differences in triacylglycerol accumulation. Additionally, Rv3272 expression protects mycobacteria from acidic, oxidative and antibiotic stress under in vitro conditions. Taken together, these studies indicate a significant role for Rv3272 in host-pathogen interaction.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
transferase activity transferase activity
Biological process: not assigned
Cellular component: not assigned
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, B
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: Probable fatty acyl-CoA transferase Rv3272
Source organism: Mycobacterium tuberculosis
Length: 394 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMPTSNPAKPLDGFRVLDFTQNVAGPLAGQVLVDLGAEVIKVEAPGGEAARQITSVLPGRPPLATYFLPNNRGKKSVTVDLTTEQAKQQMLRLADTADVVLEAFRPGTMEKLGLGPDDLRSRNPNLIYARLTAYGGNGPHGSRPGIDLVVAAEAGMTTGMPTPEGKPQIIPFQLVDNASGHVLAQAVLAALLHRERNGVADVVQVAMYDVAVGLQANQLMMHLNRAASDQPKPEPAPKAKRRKGVGFATQPSDAFRTADGYIVISAYVPKHWQKLCYLIGRPDLVEDQRFAEQRSRSINYAELTAELELALASKTATEWVQLLQANGLMACLAHTWKQVVDTPLFAENDLTLEVGRGADTITVIRTPARYASFRAVVTDPPPTAGEHNAVFLARP
UniProtKB AC: P96877 (positions: 5-394)
Coverage: 98%
Name: Probable fatty acyl-CoA transferase Rv3272
Source organism: Mycobacterium tuberculosis
Length: 394 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMPTSNPAKPLDGFRVLDFTQNVAGPLAGQVLVDLGAEVIKVEAPGGEAARQITSVLPGRPPLATYFLPNNRGKKSVTVDLTTEQAKQQMLRLADTADVVLEAFRPGTMEKLGLGPDDLRSRNPNLIYARLTAYGGNGPHGSRPGIDLVVAAEAGMTTGMPTPEGKPQIIPFQLVDNASGHVLAQAVLAALLHRERNGVADVVQVAMYDVAVGLQANQLMMHLNRAASDQPKPEPAPKAKRRKGVGFATQPSDAFRTADGYIVISAYVPKHWQKLCYLIGRPDLVEDQRFAEQRSRSINYAELTAELELALASKTATEWVQLLQANGLMACLAHTWKQVVDTPLFAENDLTLEVGRGADTITVIRTPARYASFRAVVTDPPPTAGEHNAVFLARP
UniProtKB AC: P96877 (positions: 5-393)
Coverage: 98%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: CoA-transferase family III
Evidence level: Indirect evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
The structure of CaiB reveals a spectacular fold where two monomers are interlaced to form an interlocked dimer with large interface (PMID:15518548). The folding path of CaiB and other proteins of this fold must be quite complex because the dimer cannot be formed by the individually folded monomers, partial unfolding would have to take place to break the CaiB dimer, thus it is most probably very stable (PMID:15518548).
Chain A:
N/A
Chain B:
N/A
Surface and contacts features:
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). Download the CIF file (.cif)
Download this entry's XML file (.xml)
Download this entry's JSON file (.json)
