1jw2

From Proteopedia

(Difference between revisions)

Revision as of 08:43, 21 April 2021

SOLUTION STRUCTURE OF HEMOLYSIN EXPRESSION MODULATING PROTEIN Hha FROM ESCHERICHIA COLI. Ontario Centre for Structural Proteomics target EC0308_1_72; Northeast Structural Genomics Target ET88

Structural highlights

1jw2 is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[HHA_ECOLI] Down-regulates hemolysin production and can also stimulate transposition events in vivo. Binds DNA and influences DNA topology in response to environmental stimuli. Involved in persister cell formation, acting downstream of mRNA interferase (toxin) MqsR. Decreases biofilm formation by repressing the transcription of fimbrial genes fimA and ihfA, and by repressing the transcription of tRNAs corresponding to rare codons, which are abundant in type 1 fimbrial genes.^[1] ^[2] ^[3] ^[4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The influx of genomic sequence information has led to the concept of structural proteomics, the determination of protein structures on a genome-wide scale. Here we describe an approach to structural proteomics of small proteins using NMR spectroscopy. Over 500 small proteins from several organisms were cloned, expressed, purified, and evaluated by NMR. Although there was variability among proteomes, overall 20% of these proteins were found to be readily amenable to NMR structure determination. NMR sample preparation was centralized in one facility, and a distributive approach was used for NMR data collection and analysis. Twelve structures are reported here as part of this approach, which allowed us to infer putative functions for several conserved hypothetical proteins.

An NMR approach to structural proteomics.,Yee A, Chang X, Pineda-Lucena A, Wu B, Semesi A, Le B, Ramelot T, Lee GM, Bhattacharyya S, Gutierrez P, Denisov A, Lee CH, Cort JR, Kozlov G, Liao J, Finak G, Chen L, Wishart D, Lee W, McIntosh LP, Gehring K, Kennedy MA, Edwards AM, Arrowsmith CH Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1825-30. PMID:11854485^[5]

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

References

↑ Nieto JM, Carmona M, Bolland S, Jubete Y, de la Cruz F, Juarez A. The hha gene modulates haemolysin expression in Escherichia coli. Mol Microbiol. 1991 May;5(5):1285-93. PMID:1956303
↑ Barrios AF, Zuo R, Ren D, Wood TK. Hha, YbaJ, and OmpA regulate Escherichia coli K12 biofilm formation and conjugation plasmids abolish motility. Biotechnol Bioeng. 2006 Jan 5;93(1):188-200. PMID:16317765 doi:http://dx.doi.org/10.1002/bit.20681
↑ Garcia-Contreras R, Zhang XS, Kim Y, Wood TK. Protein translation and cell death: the role of rare tRNAs in biofilm formation and in activating dormant phage killer genes. PLoS One. 2008 Jun 11;3(6):e2394. doi: 10.1371/journal.pone.0002394. PMID:18545668 doi:http://dx.doi.org/10.1371/journal.pone.0002394
↑ Kim Y, Wood TK. Toxins Hha and CspD and small RNA regulator Hfq are involved in persister cell formation through MqsR in Escherichia coli. Biochem Biophys Res Commun. 2010 Jan 1;391(1):209-13. doi:, 10.1016/j.bbrc.2009.11.033. Epub 2009 Nov 10. PMID:19909729 doi:10.1016/j.bbrc.2009.11.033
↑ Yee A, Chang X, Pineda-Lucena A, Wu B, Semesi A, Le B, Ramelot T, Lee GM, Bhattacharyya S, Gutierrez P, Denisov A, Lee CH, Cort JR, Kozlov G, Liao J, Finak G, Chen L, Wishart D, Lee W, McIntosh LP, Gehring K, Kennedy MA, Edwards AM, Arrowsmith CH. An NMR approach to structural proteomics. Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1825-30. PMID:11854485 doi:10.1073/pnas.042684599

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jw2"

@@ Line 3: / Line 3: @@
 <StructureSection load='1jw2' size='340' side='right'caption='[[1jw2]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1jw2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JW2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JW2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1jw2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JW2 FirstGlance]. <br>
-</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=1jw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jw2 OCA], [http://pdbe.org/1jw2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jw2 RCSB], [http://www.ebi.ac.uk/pdbsum/1jw2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jw2 ProSAT], [http://www.topsan.org/Proteins/NESGC/1jw2 TOPSAN]</span></td></tr>
+</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=1jw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jw2 OCA], [https://pdbe.org/1jw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jw2 RCSB], [https://www.ebi.ac.uk/pdbsum/1jw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jw2 ProSAT], [https://www.topsan.org/Proteins/NESGC/1jw2 TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HHA_ECOLI HHA_ECOLI]] Down-regulates hemolysin production and can also stimulate transposition events in vivo. Binds DNA and influences DNA topology in response to environmental stimuli. Involved in persister cell formation, acting downstream of mRNA interferase (toxin) MqsR. Decreases biofilm formation by repressing the transcription of fimbrial genes fimA and ihfA, and by repressing the transcription of tRNAs corresponding to rare codons, which are abundant in type 1 fimbrial genes.<ref>PMID:1956303</ref> <ref>PMID:16317765</ref> <ref>PMID:18545668</ref> <ref>PMID:19909729</ref>
+[[https://www.uniprot.org/uniprot/HHA_ECOLI HHA_ECOLI]] Down-regulates hemolysin production and can also stimulate transposition events in vivo. Binds DNA and influences DNA topology in response to environmental stimuli. Involved in persister cell formation, acting downstream of mRNA interferase (toxin) MqsR. Decreases biofilm formation by repressing the transcription of fimbrial genes fimA and ihfA, and by repressing the transcription of tRNAs corresponding to rare codons, which are abundant in type 1 fimbrial genes.<ref>PMID:1956303</ref> <ref>PMID:16317765</ref> <ref>PMID:18545668</ref> <ref>PMID:19909729</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1jw2

From Proteopedia

Revision as of 08:43, 21 April 2021

SOLUTION STRUCTURE OF HEMOLYSIN EXPRESSION MODULATING PROTEIN Hha FROM ESCHERICHIA COLI. Ontario Centre for Structural Proteomics target EC0308_1_72; Northeast Structural Genomics Target ET88

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox