Database accession: MF7000922
Name: Poly-HAMP domains from the P. aeruginosa soluble receptor Aer2
PDB ID: 3lnr
Experimental method: X-ray (2.64 Å)
Assembly: Homodimer
Source organism: Pseudomonas aeruginosa
Primary publication of the structure:
Airola MV, Watts KJ, Bilwes AM, Crane BR
Structure of concatenated HAMP domains provides a mechanism for signal transduction.
(2010) Structure 18: 436-48
PMID: 20399181
Abstract:
HAMP domains are widespread prokaryotic signaling modules found as single domains or poly-HAMP chains in both transmembrane and soluble proteins. The crystal structure of a three-unit poly-HAMP chain from the Pseudomonas aeruginosa soluble receptor Aer2 defines a universal parallel four-helix bundle architecture for diverse HAMP domains. Two contiguous domains integrate to form a concatenated di-HAMP structure. The three HAMP domains display two distinct conformations that differ by changes in helical register, crossing angle, and rotation. These conformations are stabilized by different subsets of conserved residues. Known signals delivered to HAMP would be expected to switch the relative stability of the two conformations and the position of a coiled-coil phase stutter at the junction with downstream helices. We propose that the two conformations represent opposing HAMP signaling states and suggest a signaling mechanism whereby HAMP domains interconvert between the two states, which alternate down a poly-HAMP chain.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
identical protein binding identical protein binding
metal ion binding metal ion binding
transmembrane signaling receptor activity transmembrane signaling receptor activity
Biological process:
aerotaxis aerotaxis
chemotaxis chemotaxis
positive aerotaxis positive aerotaxis
signal transduction signal transduction
Cellular component:
cytoplasm cytoplasm
plasma membrane plasma membrane
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, A-2
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: Methyl-accepting chemotaxis protein McpB
Source organism: Pseudomonas aeruginosa
Length: 679 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMGLFNAHAVAQQRADRIATLLQSFADGQLDTAVGEAPAPGYERLYDSLRALQRQLREQRAELQQVESLEAGLAEMSRQHEAGWIDQTIPAERLEGRAARIAKGVNELVAAHIAVKMKVVSVVTAYGQGNFEPLMDRLPGKKAQITEAIDGVRERLRGAAEATSAQLATAAYNARIKSALDNVSANVMIADNDLNIIYMNRTVSEMLGRAEADIRKQLPNFDAGRLMGANIDVFHKNPAHQRHLLANLTGVHKAELNLGGRRFSLDVVPVFNDANERLGSAVQWTDRTEEHRAEQEVSQLVQAAAAGDFSKRVEEAGKEGFFLRLAKDLNSLVDTADRGLRDVSRMLGALAQGDLTQRIEADYQGTFGQLKDFSNDTAQSLSRMLGQIREAADTINTAASEIASGNAELSARTEQQASSLEETASSMEELTSTVKLNAENARQANSLAANASEVATQGGTVVQKVVSTMSSINESARKIADIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRTLAQRSAAAAKEIKTLISDSVDKVENGNTLVAQAGQTMSDIVVAIRRVTDIMSEIAAASAEQSTGIEEVNSAVSQMDDMTQQNAALVEEAAAAAEAMQEQAGLLNQSVAVFRLDTPPSVVQLASARPSAPRPSAPAPLARSGMARASKARKEDGWEEF
UniProtKB AC: Q9I6V6 (positions: 1-157)
Coverage: 23%
Name: Methyl-accepting chemotaxis protein McpB
Source organism: Pseudomonas aeruginosa
Length: 679 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMGLFNAHAVAQQRADRIATLLQSFADGQLDTAVGEAPAPGYERLYDSLRALQRQLREQRAELQQVESLEAGLAEMSRQHEAGWIDQTIPAERLEGRAARIAKGVNELVAAHIAVKMKVVSVVTAYGQGNFEPLMDRLPGKKAQITEAIDGVRERLRGAAEATSAQLATAAYNARIKSALDNVSANVMIADNDLNIIYMNRTVSEMLGRAEADIRKQLPNFDAGRLMGANIDVFHKNPAHQRHLLANLTGVHKAELNLGGRRFSLDVVPVFNDANERLGSAVQWTDRTEEHRAEQEVSQLVQAAAAGDFSKRVEEAGKEGFFLRLAKDLNSLVDTADRGLRDVSRMLGALAQGDLTQRIEADYQGTFGQLKDFSNDTAQSLSRMLGQIREAADTINTAASEIASGNAELSARTEQQASSLEETASSMEELTSTVKLNAENARQANSLAANASEVATQGGTVVQKVVSTMSSINESARKIADIIGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRTLAQRSAAAAKEIKTLISDSVDKVENGNTLVAQAGQTMSDIVVAIRRVTDIMSEIAAASAEQSTGIEEVNSAVSQMDDMTQQNAALVEEAAAAAEAMQEQAGLLNQSVAVFRLDTPPSVVQLASARPSAPRPSAPAPLARSGMARASKARKEDGWEEF
UniProtKB AC: Q9I6V6 (positions: 1-157)
Coverage: 23%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: Methyl-accepting chemotaxis protein McpB, HAMP domains
Evidence level: Indirect evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
Aer2 1–172 is a symmetric dimer containing three HAMP domains. The basic construction unit of each HAMP domain is a monomeric unit of two parallel α-helices joined by a linker. This unit dimerizes and coils around a central supercoil axis to form a parallel four-helix bundle. The second and third HAMP domains are concatenated to form an interwoven di-HAMP structure (PMID:20399181).
Chain A:
N/A
Chain A-2:
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)
