4hi4

From Proteopedia

(Difference between revisions)

Revision as of 08:18, 3 November 2022

Crystal structure of the 5-coordinate ferric heme-binding PAS domain of Aer2 from P. aeruginosa

Structural highlights

4hi4 is a 4 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MCPB_PSEAE Chemoreceptor that plays a critical role in the virulence and pathogenesis of P.aeruginosa in a variety of hosts (PubMed:31511598). Probably acts through oxygen sensing (PubMed:31511598, PubMed:28167524, PubMed:34383467). Uses a heme-based sensor (PubMed:21255112, PubMed:22622145). Could be involved in chemotaxis (PubMed:12142407, PubMed:14987771). When expressed in E.coli, is able to sense and mediate repellent responses to oxygen, carbon monoxide and nitric oxide (PubMed:21255112).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

Publication Abstract from PubMed

Bacterial receptors typically contain modular architectures with distinct functional domains that combine to send signals in response to stimuli. Although the properties of individual components have been investigated in many contexts, there is little information about how diverse sets of modules work together in full-length receptors. Here we investigate the architecture of Aer2, a soluble gas-sensing receptor that has emerged as a model for PAS and poly-HAMP domain signaling. The crystal structure of the heme-binding PAS domain in the ferric, ligand-free form, in comparison to the previously determined cyanide-bound state,identifies conformational changes induced by ligand bindingthat are likely essential forthe signaling mechanism.Heme-pocket alternations share some similarities with the heme-based PAS sensors FixL and EcDOS, but propagate to the Ibeta-strand in a manner predicted to alter PAS-PAS associations and the downstream HAMP junction within full-length Aer2. SAXSof PAS and poly-HAMP domain fragments of increasing complexity allow unambiguous domain assignments and reveal a linear quaternary structure. The Aer2 PAS dimeric crystal structure fits well within ab initioSAXS molecular envelopes and pulsed-dipolar ESR measurements of inter-PAS distances confirm the crystallographic PAS arrangement within Aer2. Spectroscopic and pull-down assays fail to detect direct interactions between the PAS and HAMP domains. Overall, the Aer2 signaling mechanism differs from the E. coliAer paradigm, where side-on PAS-HAMP contacts are key. We propose an in-line model for Aer2 signaling, where ligand binding induces alterations in PAS domain structure and subunit association that is relayed through the poly-HAMP junction to downstream domains.

Architecture of the soluble receptor Aer2 indicates an in-line mechanism for PAS and HAMP domain signaling.,Airola MV, Huh D, Sukomon N, Widom J, Sircar R, Borbat PP, Freed JH, Watts KJ, Crane BR J Mol Biol. 2012 Dec 26. pii: S0022-2836(12)00944-8. doi:, 10.1016/j.jmb.2012.12.011. PMID:23274111^[8]

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

References

↑ Ferrandez A, Hawkins AC, Summerfield DT, Harwood CS. Cluster II che genes from Pseudomonas aeruginosa are required for an optimal chemotactic response. J Bacteriol. 2002 Aug;184(16):4374-83. PMID:12142407
↑ Hong CS, Shitashiro M, Kuroda A, Ikeda T, Takiguchi N, Ohtake H, Kato J. Chemotaxis proteins and transducers for aerotaxis in Pseudomonas aeruginosa. FEMS Microbiol Lett. 2004 Feb 16;231(2):247-52. doi:, 10.1016/S0378-1097(04)00009-6. PMID:14987771 doi:http://dx.doi.org/10.1016/S0378-1097(04)00009-6
↑ Watts KJ, Taylor BL, Johnson MS. PAS/poly-HAMP signalling in Aer-2, a soluble haem-based sensor. Mol Microbiol. 2011 Feb;79(3):686-99. doi: 10.1111/j.1365-2958.2010.07477.x. Epub, 2010 Dec 7. PMID:21255112 doi:http://dx.doi.org/10.1111/j.1365-2958.2010.07477.x
↑ Sawai H, Sugimoto H, Shiro Y, Ishikawa H, Mizutani Y, Aono S. Structural basis for oxygen sensing and signal transduction of the heme-based sensor protein Aer2 from Pseudomonas aeruginosa. Chem Commun (Camb). 2012 Jul 4;48(52):6523-5. doi: 10.1039/c2cc32549g. Epub 2012 , May 23. PMID:22622145 doi:10.1039/c2cc32549g
↑ Garcia D, Orillard E, Johnson MS, Watts KJ. Gas Sensing and Signaling in the PAS-Heme Domain of the Pseudomonas aeruginosa Aer2 Receptor. J Bacteriol. 2017 Aug 22;199(18). pii: JB.00003-17. doi: 10.1128/JB.00003-17., Print 2017 Sep 15. PMID:28167524 doi:http://dx.doi.org/10.1128/JB.00003-17
↑ Garcia-Fontana C, Vilchez JI, Gonzalez-Requena M, Gonzalez-Lopez J, Krell T, Matilla MA, Manzanera M. The involvement of McpB chemoreceptor from Pseudomonas aeruginosa PAO1 in virulence. Sci Rep. 2019 Sep 11;9(1):13166. doi: 10.1038/s41598-019-49697-7. PMID:31511598 doi:http://dx.doi.org/10.1038/s41598-019-49697-7
↑ Orillard E, Anaya S, Johnson MS, Watts KJ. Oxygen-Induced Conformational Changes in the PAS-Heme Domain of the Pseudomonas aeruginosa Aer2 Receptor. Biochemistry. 2021 Aug 31;60(34):2610-2622. doi: 10.1021/acs.biochem.1c00452., Epub 2021 Aug 12. PMID:34383467 doi:http://dx.doi.org/10.1021/acs.biochem.1c00452
↑ Airola MV, Huh D, Sukomon N, Widom J, Sircar R, Borbat PP, Freed JH, Watts KJ, Crane BR. Architecture of the soluble receptor Aer2 indicates an in-line mechanism for PAS and HAMP domain signaling. J Mol Biol. 2012 Dec 26. pii: S0022-2836(12)00944-8. doi:, 10.1016/j.jmb.2012.12.011. PMID:23274111 doi:10.1016/j.jmb.2012.12.011

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/4hi4"

Categories: Large Structures | Pseudomonas aeruginosa | Airola MV | Crane BR

@@ Line 1: / Line 1: @@
 ==Crystal structure of the 5-coordinate ferric heme-binding PAS domain of Aer2 from P. aeruginosa==
-<StructureSection load='4hi4' size='340' side='right' caption='[[4hi4]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='4hi4' size='340' side='right'caption='[[4hi4]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4hi4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HI4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HI4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4hi4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HI4 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lnr|3lnr]], [[3vol|3vol]]</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=4hi4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hi4 OCA], [https://pdbe.org/4hi4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hi4 RCSB], [https://www.ebi.ac.uk/pdbsum/4hi4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hi4 ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aer2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hi4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hi4 OCA], [http://pdbe.org/4hi4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hi4 RCSB], [http://www.ebi.ac.uk/pdbsum/4hi4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hi4 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/MCPB_PSEAE MCPB_PSEAE] Chemoreceptor that plays a critical role in the virulence and pathogenesis of P.aeruginosa in a variety of hosts (PubMed:31511598). Probably acts through oxygen sensing (PubMed:31511598, PubMed:28167524, PubMed:34383467). Uses a heme-based sensor (PubMed:21255112, PubMed:22622145). Could be involved in chemotaxis (PubMed:12142407, PubMed:14987771). When expressed in E.coli, is able to sense and mediate repellent responses to oxygen, carbon monoxide and nitric oxide (PubMed:21255112).<ref>PMID:12142407</ref> <ref>PMID:14987771</ref> <ref>PMID:21255112</ref> <ref>PMID:22622145</ref> <ref>PMID:28167524</ref> <ref>PMID:31511598</ref> <ref>PMID:34383467</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Airola, M V]]
+[[Category: Large Structures]]
-[[Category: Crane, B R]]
+[[Category: Pseudomonas aeruginosa]]
-[[Category: Diatomic gas sensor]]
+[[Category: Airola MV]]
-[[Category: Pas domain]]
+[[Category: Crane BR]]
-[[Category: Signaling protein]]

4hi4

From Proteopedia

Revision as of 08:18, 3 November 2022

Crystal structure of the 5-coordinate ferric heme-binding PAS domain of Aer2 from P. aeruginosa

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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