6igb: Difference between revisions

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New page: '''Unreleased structure''' The entry 6igb is ON HOLD Authors: Song, Y.J., Shen, Y.L., Wang, K.L., Li, T., Zhu, Y.B., Li, C.C., He, L.H., Zhao, N.L., Zhao, C., Yang, J., Huang, Q., Mu, X...
 
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'''Unreleased structure'''


The entry 6igb is ON HOLD
==the structure of Pseudomonas aeruginosa Periplasmic gluconolactonase, PpgL==
<StructureSection load='6igb' size='340' side='right'caption='[[6igb]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6igb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IGB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IGB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.651&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6igb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6igb OCA], [https://pdbe.org/6igb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6igb RCSB], [https://www.ebi.ac.uk/pdbsum/6igb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6igb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9HWH7_PSEAE Q9HWH7_PSEAE]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Biofilm formation is a critical determinant in the pathopoiesis of Pseudomonas aeruginosa It could significantly increase bacterial resistance to drugs and host defense. Thus, inhibition of biofilm matrix production could be regarded as a promising attempt to prevent colonization of P. aeruginosa and the subsequent infection. PpgL, a periplasmic gluconolactonase, has been reported to be involved in P. aeruginosa quorum-sensing (QS) system regulation. However, the detailed function and catalysis mechanism remain elusive. Here, the crystal structure of PpgL is described in the current study, along with biochemical analysis, revealing that PpgL is a typical beta-propeller enzyme with unique metal-independent lactone hydrolysis activity. Consequently, comparative analysis of seven-bladed propeller lactone-catalyzing enzymes and mutagenesis studies identify the critical sites which contribute to the diverse catalytic and substrate recognition functions. In addition, the reduced biofilm formation and attenuated invasion phenotype resulting from deletion of ppgL confirm the importance of PpgL in P. aeruginosa pathogenesis. These results suggest that PpgL is a potential target for developing new agents against the diseases caused by P. aeruginosa.


Authors: Song, Y.J., Shen, Y.L., Wang, K.L., Li, T., Zhu, Y.B., Li, C.C., He, L.H., Zhao, N.L., Zhao, C., Yang, J., Huang, Q., Mu, X.Y.
Structural and Functional Insights into PpgL, a Metal-Independent beta-Propeller Gluconolactonase That Contributes to Pseudomonas aeruginosa Virulence.,Song YJ, Wang KL, Shen YL, Gao J, Li T, Zhu YB, Li CC, He LH, Zhou QX, Zhao NL, Zhao C, Yang J, Huang Q, Mu XY, Li H, Dou DF, Liu C, He JH, Sun B, Bao R Infect Immun. 2019 Mar 25;87(4). pii: IAI.00847-18. doi: 10.1128/IAI.00847-18., Print 2019 Apr. PMID:30642898<ref>PMID:30642898</ref>


Description: the structure of Pseudomonas aeruginosa Periplasmic gluconolactonase, PpgL
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Li, C.C]]
<div class="pdbe-citations 6igb" style="background-color:#fffaf0;"></div>
[[Category: Shen, Y.L]]
== References ==
[[Category: Huang, Q]]
<references/>
[[Category: Yang, J]]
__TOC__
[[Category: Zhao, C]]
</StructureSection>
[[Category: He, L.H]]
[[Category: Large Structures]]
[[Category: Song, Y.J]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Zhao, N.L]]
[[Category: He LH]]
[[Category: Mu, X.Y]]
[[Category: Huang Q]]
[[Category: Li, T]]
[[Category: Li CC]]
[[Category: Wang, K.L]]
[[Category: Li T]]
[[Category: Zhu, Y.B]]
[[Category: Mu XY]]
[[Category: Shen YL]]
[[Category: Song YJ]]
[[Category: Wang KL]]
[[Category: Yang J]]
[[Category: Zhao C]]
[[Category: Zhao NL]]
[[Category: Zhu YB]]

Latest revision as of 12:40, 22 November 2023

the structure of Pseudomonas aeruginosa Periplasmic gluconolactonase, PpgLthe structure of Pseudomonas aeruginosa Periplasmic gluconolactonase, PpgL

Structural highlights

6igb is a 2 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.651Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9HWH7_PSEAE

Publication Abstract from PubMed

Biofilm formation is a critical determinant in the pathopoiesis of Pseudomonas aeruginosa It could significantly increase bacterial resistance to drugs and host defense. Thus, inhibition of biofilm matrix production could be regarded as a promising attempt to prevent colonization of P. aeruginosa and the subsequent infection. PpgL, a periplasmic gluconolactonase, has been reported to be involved in P. aeruginosa quorum-sensing (QS) system regulation. However, the detailed function and catalysis mechanism remain elusive. Here, the crystal structure of PpgL is described in the current study, along with biochemical analysis, revealing that PpgL is a typical beta-propeller enzyme with unique metal-independent lactone hydrolysis activity. Consequently, comparative analysis of seven-bladed propeller lactone-catalyzing enzymes and mutagenesis studies identify the critical sites which contribute to the diverse catalytic and substrate recognition functions. In addition, the reduced biofilm formation and attenuated invasion phenotype resulting from deletion of ppgL confirm the importance of PpgL in P. aeruginosa pathogenesis. These results suggest that PpgL is a potential target for developing new agents against the diseases caused by P. aeruginosa.

Structural and Functional Insights into PpgL, a Metal-Independent beta-Propeller Gluconolactonase That Contributes to Pseudomonas aeruginosa Virulence.,Song YJ, Wang KL, Shen YL, Gao J, Li T, Zhu YB, Li CC, He LH, Zhou QX, Zhao NL, Zhao C, Yang J, Huang Q, Mu XY, Li H, Dou DF, Liu C, He JH, Sun B, Bao R Infect Immun. 2019 Mar 25;87(4). pii: IAI.00847-18. doi: 10.1128/IAI.00847-18., Print 2019 Apr. PMID:30642898[1]

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

References

  1. Song YJ, Wang KL, Shen YL, Gao J, Li T, Zhu YB, Li CC, He LH, Zhou QX, Zhao NL, Zhao C, Yang J, Huang Q, Mu XY, Li H, Dou DF, Liu C, He JH, Sun B, Bao R. Structural and Functional Insights into PpgL, a Metal-Independent beta-Propeller Gluconolactonase That Contributes to Pseudomonas aeruginosa Virulence. Infect Immun. 2019 Mar 25;87(4). pii: IAI.00847-18. doi: 10.1128/IAI.00847-18., Print 2019 Apr. PMID:30642898 doi:http://dx.doi.org/10.1128/IAI.00847-18

6igb, resolution 1.65Å

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