F(M197)H mutant structure of Photosynthetic Reaction Center From Rhodobacter Sphaeroides strain RV by fixed-target serial synchrotron crystallography (room temperature, 26keV). Determined by X-ray diffraction at 2.04 Å resolution. Released 27 Apr 2022.
Explore 7P2C in 3D Show helices and sheets RCSB PDB PDBe
7P2C contains 48 α-helices and 32 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-34 | 23 | |
| β-strand | 43 | 1 | 1 |
| β-strand | 49 | 1 | 1 |
| α-helix | 50 | 1 | |
| α-helix | 57-61 | 5 | |
| β-strand | 62-65 | 4 | 2 |
| β-strand | 72-75 | 4 | 2 |
| β-strand | 87-89 | 3 | 3 |
| β-strand | 98-100 | 3 | 3 |
| α-helix | 104-107 | 4 | |
| α-helix | 110-112 | 3 | |
| β-strand | 123 | 1 | 4 |
| β-strand | 129 | 1 | 4 |
| β-strand | 131-133 | 3 | 5 |
| α-helix | 134-136 | 3 | |
| β-strand | 141-144 | 4 | 6 |
| β-strand | 152-154 | 3 | 5 |
| β-strand | 160-170 | 11 | 5 |
| β-strand | 175-183 | 9 | 5 |
| β-strand | 188-192 | 5 | 5 |
| α-helix | 193-195 | 3 | |
| β-strand | 197-198 | 2 | 5 |
| β-strand | 203-204 | 2 | 5 |
| α-helix | 210-215 | 6 | |
| α-helix | 217-219 | 3 | |
| β-strand | 221 | 1 | 7 |
| β-strand | 224 | 1 | 7 |
| α-helix | 227-243 | 17 | |
| α-helix | 245-247 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 1 |
| α-helix | 7-9 | 3 | |
| β-strand | 25-26 | 2 | 8 |
| β-strand | 29-30 | 2 | 8 |
| α-helix | 32-56 | 25 | |
| β-strand | 65-66 | 2 | 9 |
| α-helix | 67-70 | 4 | |
| α-helix | 71-73 | 3 | |
| α-helix | 80-82 | 3 | |
| α-helix | 84-111 | 28 | |
| α-helix | 116-129 | 14 | |
| α-helix | 130-134 | 5 | |
| α-helix | 135-139 | 5 | |
| α-helix | 142-144 | 3 | |
| α-helix | 146-147 | 2 | |
| β-strand | 148-149 | 2 | 9 |
| α-helix | 152-163 | 12 | |
| α-helix | 167-169 | 3 | |
| α-helix | 171-198 | 28 | |
| α-helix | 209-220 | 12 | |
| α-helix | 226-249 | 24 | |
| β-strand | 251 | 1 | 10 |
| β-strand | 255 | 1 | 10 |
| α-helix | 259-262 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-13 | 3 | 6 |
| α-helix | 26-28 | 3 | |
| β-strand | 29 | 1 | 11 |
| α-helix | 39-41 | 3 | |
| β-strand | 51 | 1 | 11 |
| α-helix | 53-77 | 25 | |
| α-helix | 82-87 | 6 | |
| β-strand | 94 | 1 | 12 |
| α-helix | 95-98 | 4 | |
| α-helix | 99-101 | 3 | |
| α-helix | 109-111 | 3 | |
| α-helix | 113-139 | 27 | |
| α-helix | 145-158 | 14 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-168 | 5 | |
| α-helix | 171-173 | 3 | |
| β-strand | 177 | 1 | 12 |
| α-helix | 179-192 | 14 | |
| α-helix | 196-198 | 3 | |
| α-helix | 200-225 | 26 | |
| α-helix | 227-229 | 3 | |
| α-helix | 234-239 | 6 | |
| α-helix | 243-256 | 14 | |
| α-helix | 264-285 | 22 | |
| β-strand | 287 | 1 | 13 |
| β-strand | 291 | 1 | 13 |
| α-helix | 294-300 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Reaction center protein H chain | H | protein | 242 | Rhodobacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) | Q3J170 (AlphaFold model) |
| Reaction center protein L chain | L | protein | 281 | Rhodobacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) | Q3J1A5 (AlphaFold model) |
| Reaction center protein M chain | M | protein | 303 | Rhodobacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) | Q3J1A6 (AlphaFold model) |
>7P2C_1 Reaction center protein H chain (chains H) NFDLASLAIYSFWIFLAGLIYYLQTENMREGYPLENEDGTPAANQGPFPLPKPKTFILPH GRGTLTVPGPESEDRPIALARTAVSEGFPHAPTGDPMKDGVGPASWVARRDLPELDGHGH NKIKPMKAAAGFHVSAGKNPIGLPVRGCDLEIAGKVVDIWVDIPEQMARFLEVELKDGST RLLPMQMVKVQSNRVHVNALSSDLFAGIPTIKSPTEVTLLEEDKICGYVAGGLMYAAPKR KS
>7P2C_2 Reaction center protein L chain (chains L) ALLSFERKYRVPGGTLVGGNLFDFWVGPFYVGFFGVATFFFAALGIILIAWSAVLQGTWN PQLISVYPPALEYGLGGAPLAKGGLWQIITICATGAFVSWALREVEICRKLGIGYHIPFA FAFAILAYLTLVLFRPVMMGAWGYAFPYGIWTHLDWVSNTGYTYGNFHYNPAHMIAITFF FTNALALALHGALVLSAANPEKGKEMRTPDHEDTFFRDLVGYSIGTLGIHRLGLLLSLSA VFFSALCMIITGTIWFDQWVDWWQWWVKLPWWANIPGGING
>7P2C_3 Reaction center protein M chain (chains M) AEYQNIFTQVQVRGPADLGMTEDVNLANRSGVGPFSTLLGWFGNAQLGPIYLGSLGVLSL FSGLMWFFTIGIWFWYQAGWNPAVFLRDLFFFSLEPPAPEYGLSFAAPLKEGGLWLIASF FMFVAVWSWWGRTYLRAQALGMGKHTAWAFLSAIWLWMVLGFIRPILMGSWSEAVPYGIF SHLDWTNNFSLVHGNLHYNPFHGLSIAFLYGSALLFAMHGATILAVSRFGGERELEQIAD RGTAAERAALFWRWTMGFNATMEGIHRWAIWMAVLVTLTGGIGILLSGTVVDNWYVWGQN HGM
| ID | Name | Formula | Copies |
|---|---|---|---|
| NKP | (2R)-2-hydroxy-3-(phosphonooxy)propyl (9E)-octadec-9-enoate | C21 H41 O7 P | 2 |
| BPH | Bacteriopheophytin a | C55 H76 N4 O6 | 2 |
| BCL | Bacteriochlorophyll a | C55 H74 Mg N4 O6 | 4 |
| MYS | Pentadecane | C15 H32 | 3 |
| OLC | (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate | C21 H40 O4 | 1 |
| LDA | Lauryl dimethylamine-N-oxide | C14 H31 N O | 2 |
| PO4 | Phosphate ion | O4 P | 1 |
| SPN | Speroidenone | C41 H70 O2 | 1 |
| FE | FE (III) ion | Fe | 1 |
| U10 | Ubiquinone-10 | C59 H90 O4 | 1 |
Water and common crystallization additives (EDO) are not listed.
X-ray structure of the Rhodobacter sphaeroides reaction center with an M197 Phe→His substitution clarifies the properties of the mutant complex. Selikhanov, G., Fufina, T., Guenther, S. et al. IUCrJ (2022) 9:261-271. DOI 10.1107/S2052252521013178 · PubMed
Other PDB entries of the same protein (UniProt Q3J170 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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