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7t51

From Proteopedia

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Crystal structure of the molybdate-binding periplasmic protein ModA from the bacteria Pseudomonsa aeruginosa in molybdate-bound form

Structural highlights

7t51 is a 2 chain structure with sequence from Pseudomonas aeruginosa PA1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MODA_PSEAE Part of the ABC transporter complex ModABC involved in the transport of molybdenum into the cell (Probable). Binds tungstate and molybdate (PubMed:31627455, PubMed:25172858). Can also bind chromate, with lower affinity (PubMed:31627455). Plays an essential role in recruitment of molybdate for nitrate reduction (PubMed:25172858).^[1] ^[2] ^[3]

Publication Abstract from PubMed

Acquisition of the trace-element molybdenum via the high-affinity ATP-binding cassette permease ModABC is essential for Pseudomonas aeruginosa respiration in anaerobic and microaerophilic environments. This study determined the X-ray crystal structures of the molybdenum-recruiting solute-binding protein ModA from P. aeruginosa PAO1 in the metal-free state and bound to the group 6 metal oxyanions molybdate, tungstate, and chromate. Pseudomonas aeruginosa PAO1 ModA has a non-contiguous dual-hinged bilobal structure with a single metal-binding site positioned between the two domains. Metal binding results in a 22 degrees relative rotation of the two lobes with the oxyanions coordinated by four residues, that contribute six hydrogen bonds, distinct from ModA orthologues that feature an additional oxyanion-binding residue. Analysis of 485 Pseudomonas ModA sequences revealed conservation of the metal-binding residues and beta-sheet structural elements, highlighting their contribution to protein structure and function. Despite the capacity of ModA to bind chromate, deletion of modA did not affect P. aeruginosa PAO1 sensitivity to chromate toxicity nor impact cellular accumulation of chromate. Exposure to sub-inhibitory concentrations of chromate broadly perturbed P. aeruginosa metal homeostasis and, unexpectedly, was associated with an increase in ModA-mediated molybdenum uptake. Elemental analyses of the proteome from anaerobically grown P. aeruginosa revealed that, despite the increase in cellular molybdenum upon chromate exposure, distribution of the metal within the proteome was substantially perturbed. This suggested that molybdoprotein cofactor acquisition may be disrupted, consistent with the potent toxicity of chromate under anaerobic conditions. Collectively, these data reveal a complex relationship between chromate toxicity, molybdenum homeostasis and anaerobic respiration.

The Impact of Chromate on Pseudomonas aeruginosa Molybdenum Homeostasis.,Maunders EA, Ngu DHY, Ganio K, Hossain SI, Lim BYJ, Leeming MG, Luo Z, Tan A, Deplazes E, Kobe B, McDevitt CA Front Microbiol. 2022 May 24;13:903146. doi: 10.3389/fmicb.2022.903146., eCollection 2022. PMID:35685933^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Pederick VG, Eijkelkamp BA, Ween MP, Begg SL, Paton JC, McDevitt CA. Acquisition and role of molybdate in Pseudomonas aeruginosa. Appl Environ Microbiol. 2014 Nov;80(21):6843-52. PMID:25172858 doi:10.1128/AEM.02465-14
↑ Fernández M, Rico-Jiménez M, Ortega Á, Daddaoua A, García García AI, Martín-Mora D, Torres NM, Tajuelo A, Matilla MA, Krell T. Determination of Ligand Profiles for Pseudomonas aeruginosa Solute Binding Proteins. Int J Mol Sci. 2019 Oct 17;20(20):5156. PMID:31627455 doi:10.3390/ijms20205156
↑ Pederick VG, Eijkelkamp BA, Ween MP, Begg SL, Paton JC, McDevitt CA. Acquisition and role of molybdate in Pseudomonas aeruginosa. Appl Environ Microbiol. 2014 Nov;80(21):6843-52. PMID:25172858 doi:10.1128/AEM.02465-14
↑ Maunders EA, Ngu DHY, Ganio K, Hossain SI, Lim BYJ, Leeming MG, Luo Z, Tan A, Deplazes E, Kobe B, McDevitt CA. The Impact of Chromate on Pseudomonas aeruginosa Molybdenum Homeostasis. Front Microbiol. 2022 May 24;13:903146. doi: 10.3389/fmicb.2022.903146., eCollection 2022. PMID:35685933 doi:http://dx.doi.org/10.3389/fmicb.2022.903146

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7t51"

@@ Line 3: / Line 3: @@
 <StructureSection load='7t51' size='340' side='right'caption='[[7t51]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7t51]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7T51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7T51 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7t51]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PA1 Pseudomonas aeruginosa PA1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7T51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7T51 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MOO:MOLYBDATE+ION'>MOO</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7t4z|7t4z]], [[7t50|7t50]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MOO:MOLYBDATE+ION'>MOO</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7t51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7t51 OCA], [https://pdbe.org/7t51 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7t51 RCSB], [https://www.ebi.ac.uk/pdbsum/7t51 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7t51 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/MODA_PSEAE MODA_PSEAE] Part of the ABC transporter complex ModABC involved in the transport of molybdenum into the cell (Probable). Binds tungstate and molybdate (PubMed:31627455, PubMed:25172858). Can also bind chromate, with lower affinity (PubMed:31627455). Plays an essential role in recruitment of molybdate for nitrate reduction (PubMed:25172858).<ref>PMID:25172858</ref> <ref>PMID:31627455</ref> <ref>PMID:25172858</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 24: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Kobe, B]]
+[[Category: Pseudomonas aeruginosa PA1]]
-[[Category: Lim, B Y.J]]
+[[Category: Kobe B]]
-[[Category: Luo, Z]]
+[[Category: Lim BYJ]]
-[[Category: Ngu, D H.Y]]
+[[Category: Luo Z]]
-[[Category: Metal binding protein]]
+[[Category: Ngu DHY]]
-[[Category: Molybdate-binding periplasmic protein]]

7t51

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Current revision

Crystal structure of the molybdate-binding periplasmic protein ModA from the bacteria Pseudomonsa aeruginosa in molybdate-bound form

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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