| Structural highlights
6zhf is a 1 chain structure with sequence from "bacterium_monocytogenes_hominis"_nyfeldt_1932 "bacterium monocytogenes hominis" nyfeldt 1932. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | BEF, MG |
| Gene: | A3R04_02860, A7B93_02035, A7E37_07960, A7T84_03145, A8N46_03115, A9303_08250, AA141_02585, AA38_03115, AA57_04345, AA58_04340, AAT23_05730, AAT89_01270, AAV13_08720, AC638_15100, ACX75_14550, AD67_04590, ADT87_13595, AE163_09080, AE275_03115, AF000_06545, AF016_12590, AF040_14630, AF045_14565, AF209_04695, AF234_14885, AFS24_04345, AFT50_03135, AFU02_10535, AFU61_04345, AFW07_04365, AFW50_00270, AFW67_02600, AFW77_02595, AFW96_04345, AFY00_02970, AFY08_04620, AFY14_04625, AK14_13510, AL416_02600, ALZ22_03115, AO083_04340, AOA99_03360, AOX92_14460, AOX97_03115, APD69_03345, APD94_04680, APE52_04350, APE55_04330, APE78_08730, APE79_10640, APS82_08405, APY22_11485, APY32_10565, AR034_01900, AR095_04345, ARG48_02025, ARG59_04340, ARG63_02035, ARG65_02035, ARG77_04695, ARG88_04330, ARH36_03115, ARH47_03115, ARH65_03115, ARK03_06875, ARQ26_09135, ARS01_02200, ARS03_11205, ARS22_01415, ARS28_14570, ARS93_04670, ART37_07935, ARX30_08235, ARX42_11895, ARX92_07785, ARY16_02855, ARZ28_06760, ARZ35_04215, AX342_04340, B1O05_03115, B1O10_11590, B1O28_10515, B4X86_08480, B6N70_00210, BG061_14125, BG923_10000, BGC67_07100, BHE45_01350, BHY47_13215, D1B71_01000, D3132_13730, D3B94_03440, D8W60_04330, DC65_04595, DRA50_03655, E0I17_04300, E0I30_11095, E0U16_02120, E1003_07560, E1013_04820, E1027_03585, E1029_14335, E1043_09385, E1052_08335, E1312_04595, E1520_02235, E1984_14165, E1P51_04330, E1P72_02110, E1S82_14615, E1S83_04140, E1S89_01415, E1S94_10525, E1T01_09845, E1T18_01060, E1T34_01085, E1T48_04575, E1T74_10380, E1U30_14270, E1U44_07385, E1U67_11485, E1U91_11060, E1V18_11470, E1V41_12830, E1V44_01000, E1V46_01695, E1V59_10805, E1V65_07835, E1V69_04540, E1W03_01325, E1W46_07930, E1W58_07000, E1W61_04670, E1W84_05640, E1X50_00065, E1X55_00065, E1X60_00065, E1X63_00065, E1X65_10050, E1X77_00065, E1Y04_07980, E1Y22_07260, E1Y36_10040, E1Y39_06885, E1Y54_04665, E1Y60_14085, E1Y76_10360, E1Y85_07210, E1Y87_04560, E1Z07_06265, E1Z13_07150, E1Z38_04405, E1Z70_06110, E1Z81_11410, E1Z94_06145, E2B22_10915, E2B94_09335, E2G00_14170, E3362_01060, E3W12_04070, E3W83_06115, E3Y59_01330, EFC17_14975, EFC32_14240, EHH67_01225, EID73_03115, EID74_03115, EL440_01100, ELF21_11070, ELL77_14930, EON24_08110, EVB16_07950, EVC89_14095, EX531_05960, EYJ23_03110, EYJ25_09250, EZ544_07110, EZ549_04550, EZ567_04430, EZ579_10250, EZ585_00065, EZJ50_04320, F2B64_09785, F9O35_02210, FDO43_01425, FDP94_12205, FJL09_07065, FJL15_09360, FJL32_05590, FJL36_07055, FJU16_09110, FL790_12360, FMU94_04385, FMZ78_07455, FORC68_0870, FPD59_04610, FR205_09240, FR217_09360, GCV90_03275, GT55_11320, GU61_02025, GU73_02025, GX56_09050, GX92_03115, GY66_03115, GY90_03605, HL26_09525, HL28_10595, HN15_02035, IA39_04370, ID69_03115, IU04_04610, IX93_03955, JJ01_03115, JL21_03115, JU65_09035, LJ99_03115, MY31_04390, NB32_00070, NB83_10590, NI81_01900, OJ48_06380, Q842_09175, Q988_10290, R014_10950, R016_03115, RI86_13235, SH19_04830, TS11_06645, TS76_03180, TS78_02750, TX39_14805, TX56_02090, TX65_02090, UA79_03115, UL23_02205, UL40_07420, UL41_04355, WN76_13220, X855_03115, XN56_04310, XN57_03335, XN85_12310, XN87_03395, Y170_01010, Y243_04300, Y473_03115, Y519_03115, Y529_03115, Z603_10025, Z676_02255, Z689_01060 ("Bacterium monocytogenes hominis" Nyfeldt 1932) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Publication Abstract from PubMed
Many bacteria export intracellular calcium using active transporters homologous to the sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA). Here we present three crystal structures of Ca(2+)-ATPase 1 from Listeria monocytogenes (LMCA1). Structures with BeF3(-) mimicking a phosphoenzyme state reveal a closed state, which is intermediate between the outward-open E2P and the proton-occluded E2-P* conformations known for SERCA. It suggests that LMCA1 in the E2P state is pre-organized for dephosphorylation upon Ca(2+) release, consistent with the rapid dephosphorylation observed in single-molecule studies. An arginine side-chain occupies the position equivalent to calcium binding site I in SERCA, leaving a single Ca(2+)-binding site in LMCA1, corresponding to SERCA site II. Observing no putative transport pathways dedicated to protons, we infer a direct proton counter transport through the Ca(2+) exchange pathways. The LMCA1 structures provide insight into the evolutionary divergence and conserved features of this important class of ion transporters.
The crystal structure of the Ca(2+)-ATPase 1 from Listeria monocytogenes reveals a pump primed for dephosphorylation.,Basse Hansen S, Dyla M, Neumann C, Meldgaard Hoegh Quistgaard E, Lauwring Andersen J, Kjaergaard M, Nissen P J Mol Biol. 2021 Apr 29:167015. doi: 10.1016/j.jmb.2021.167015. PMID:33933469[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Basse Hansen S, Dyla M, Neumann C, Meldgaard Hoegh Quistgaard E, Lauwring Andersen J, Kjaergaard M, Nissen P. The crystal structure of the Ca(2+)-ATPase 1 from Listeria monocytogenes reveals a pump primed for dephosphorylation. J Mol Biol. 2021 Apr 29:167015. doi: 10.1016/j.jmb.2021.167015. PMID:33933469 doi:https://dx.doi.org/10.1016/j.jmb.2021.167015
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