2RCR,3D38,1EYS


Conserved Protein Domain Family
Photo-RC_L

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cd09290: Photo-RC_L 
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Subunit L of bacterial photosynthetic reaction center
Bacterial photosynthetic reaction center (RC) complex, subunit L. The bacterial photosynthetic reaction center couples light-induced electron transfer with pumping protons across the membrane using reactions involving a quinone molecule (QB) that binds two electrons and two protons at the active site. The reaction center consists of three membrane-bound subunits, designated L, M, and H, plus an additional extracellular cytochrome subunit. The L and M subunits are arranged around an axis of 2-fold rotational symmetry perpendicular to the membrane, forming a scaffold that maintains the cofactors in a precise configuration. The L and M subunits have both sequence and structural similarity, suggesting a common evolutionary origin. The L and M subunits bind noncovalently to the nine cofactors in 2-fold symmetric branches: four bacteriochlorophylls (Bchl), two bacteriopheophytins (Bphe), two ubiquinone molecules (QA and QB), and a non-heme iron. Two Bchls on the periplasmic side of the membrane form the 'special pair' or dimer which is the primary electron donor for the photosynthetic reactions. The electron transfer reaction proceeds from the dimer to an intermediate acceptor (PA), a primary quinone (QA), and a secondary quinone (QB). Protons are translocated from the bacterial cytoplasm to the periplasmic space, generating an electrochemical gradient of protons (the protonmotive force) that can be used to power reactions such as ATP synthesis. The RC complex is found in photosynthetic bacteria, such as purple bacteria and other proteobacteria species.
Statistics
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PSSM-Id: 187748
Aligned: 7 rows
Threshold Bit Score: 389.108
Created: 27-Sep-2010
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
  next features
Conserved site includes 34 residues -Click on image for an interactive view with Cn3D
Feature 1:bacteriochlorophyll binding site
Evidence:
  • Structure:1EYS_L; Thermochromatium tepidum reaction center binds four molecules of bacteriochlorophyll a, defined using 4.0 A contacts.
  • Comment:The RC requires nine co-factors: four Bchl, two Bphe, two ubiquinone and one Fe++.
  • Citation:PMID 2036405
  • Citation:PMID 8034032
  • Citation:PMID 8027023

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                         #  #                           
2RCR_L         1 ALLSFERKYRVPGGTLV----GGNLFDFWVGPFYVGFFGVATFFFAALGIILIAWSAVlq--------gtWNPQLISVYP 68  Rhodobacter sph...
3D38_L         1 ALLSFERKYRVRGGTLI----GGDLFDFWVGPYFVGFFGVSAIFFIFLGVSLIGYAASqg--------ptWDPFAISINP 68  Blastochloris v...
1EYS_L         1 AMLSFEKKYRVRGGTLI----GGDLFDFWVGPFYVGFFGVVGFCFTLLGVLLIVWGATigptgptsdlqtYNLWRISIAP 76  Thermochromatiu...
Q83XD0        35 PFSIIEEFYKRPGKTLAarffGVDPFDFWIGRFYVGLFGAISIIGIILGVAFYLYEGVvne-------gtLNILAMRIEP 107 Roseiflexus cas...
O30843         2 SMLSFEKRYRVRGGTLI----GGDLFDFWVGPFYVGFFGVLTAFFALLGTLLIVWGAAmg--------ptWNIWQISINP 69  Ectothiorhodosp...
YP_001634673  32 TIEEIEPEYKIKGRTTFsaifRYDPFDFWVGPFYVGFWGFVSVIGIIFGSYFYINETIlkgpy---sipqNFFAGRIDPP 108 Chloroflexus au...
P51760         2 AMLSFEKKYRVRGGTLV----GGDLFDFWVGPFYVGFFGVTTLFFSVLGTALIIWGASqg--------ptWNLWQISIAP 69  Rubrivivax gela...
Feature 1                                    #                          #  ##  #              #  
2RCR_L        69 PALEYGLGGAPLAKGGLWQIITICATGAFVSWALREVEICRKLGIGYHIPFAFAFAILAYLTLVLFRPVMMGAWGYAFPY 148 Rhodobacter sph...
3D38_L        69 PDLKYGLGAAPLLEGGFWQAITVCALGAFISWMLREVEISRKLGIGWHVPLAFCVPIFMFCVLQVFRPLLLGSWGHAFPY 148 Blastochloris v...
1EYS_L        77 PDLSYGLRMAPLTEGGLWQIITICAAGAFISWALREVEICRKLGIGFHVPFAFSFAIGAYLVLVFVRPLLMGAWGHGFPY 156 Thermochromatiu...
Q83XD0       108 PPVSQGLNVDPAQPGFFWFLTMVAATIAFVGWLLRQIDISLKLDMGMEVPIAFGAVVSSWITLQWLRPIAMGAWGHGFPL 187 Roseiflexus cas...
O30843        70 PDLSYGLGFAPLTEGGLWQMITICALGAFVSWALRQAEIARKLGMGLHLPIAFSVAVFAYFTLVVIRPVLLGAWGHGFPY 149 Ectothiorhodosp...
YP_001634673 109 PPELGLGFAAPGEPGFAWQMTVLFATIAFFGWMMRQVDISMKLDMGYHVPIAFGVAFSAWLVLQVIRPIALGMWHEGFVL 188 Chloroflexus au...
P51760        70 PDLKYGLGVAPLMEGGLWQIITVCAIGAFVSWALREVEICRKLGMQYHVPIAFSFAILAYVTLVVIRPILMGAWGHGFPY 149 Rubrivivax gela...
Feature 1         ## ## ### ###    ##    ## ### ###  #                                  #        
2RCR_L       149 GIWTHLDWVSNTGYTYGNFHYnPAHMIAISFFFTNALALALHGALVLSAANPEkgkemRTPDHEDTFFRDLVGYSIGTLG 228 Rhodobacter sph...
3D38_L       149 GILSHLDWVNNFGYQYLNWHYnPGHMSSVSFLFVNAMALGLHGGLILSVANPGdgdkvKTAEHENQYFRDVVGYSIGALS 228 Blastochloris v...
1EYS_L       157 GILSHLDWVSNVGYQFLHFHYnPAHMLAISFFFTNCLALSMHGSLILSVTNPQrgepvKTSEHENTFFRDIVGYSIGALA 236 Thermochromatiu...
Q83XD0       188 GITHHLDWVSNIGYQYYNFFYnPFHAIGITLLFASTLFLHMHGSAVLSEAKRN-----ISDQNIHVFWRNILGYSIGEIG 262 Roseiflexus cas...
O30843       150 GIMSHLDWVSNTGYQFLHFHYnPAHMLAIAFFFTTALALSLHGGLILSATNPKkgepvKTPEYEDTFFRDVVGYSIGALG 229 Ectothiorhodosp...
YP_001634673 189 GIMPHLDWVSNFGYRYNNFFYnPFHAIGITGLFASTWLLACHGSLILSAAQYRg---pEGGDIENVFFRDVQYYSVGESG 265 Chloroflexus au...
P51760       150 GIFSHLDWVSNVGYQYLHFHYnPAHMLAITFFFTTTLAMSMHGGLILSAANPKkgepmKTTDHEDTFFRDAVGYSIGSLG 229 Rubrivivax gela...
Feature 1                       ## ##                        
2RCR_L       229 IHRLGLLLSLSAVFFSALCMIITGTIWFDqWVDWWQWWVKLPWW 272 Rhodobacter sphaeroides
3D38_L       229 IHRLGLFLASNIFLTGAFGTIASGPFWTRgWPEWWGWWLDIPFW 272 Blastochloris viridis
1EYS_L       237 IHRLGLFLALSAAFWSAVCILISGPFWTRgWPEWWNWWLELPLW 280 Thermochromatium tepidum
Q83XD0       263 IHRVAFWTGAASVLFSNLCIFLSGTFVKD-WNAFWGFWDKMPIW 305 Roseiflexus castenholzii
O30843       230 IHRLGLFLALSAAFWSAVCIVISGPFWTQsWPEWWNWWLDLPIW 273 Ectothiorhodospira shaposhnikovii
YP_001634673 266 VHRLGYIFAIGGILSADLCILLSGWPVQD-WVSFWNFWNNLPFW 308 Chloroflexus aurantiacus J-10-fl
P51760       230 IHRLGLFLALSAAFWSAVCIVISGPFWTRgWPEWWGWWLNLPIW 273 Rubrivivax gelatinosus

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