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==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==
==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==
<StructureSection load='1jw2' size='340' side='right'caption='[[1jw2]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='1jw2' size='340' side='right'caption='[[1jw2]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[1jw2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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'>[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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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>
</table>
== Function ==
== Function ==
[[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>
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jw2 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jw2 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:11854485</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1jw2" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Chang, X]]
[[Category: Chang X]]
[[Category: Edwards, A M]]
[[Category: Edwards AM]]
[[Category: Structural genomic]]
[[Category: Savchenko A]]
[[Category: Savchenko, A]]
[[Category: Yee A]]
[[Category: Yee, A]]
[[Category: Gene regulation]]
[[Category: Hemolysin expression modulating protein]]
[[Category: Hha]]
[[Category: Nesg]]
[[Category: Ocsp]]
[[Category: PSI, Protein structure initiative]]

Revision as of 07:55, 3 April 2024

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

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