1mjc

<StructureSection load='1mjc' size='340' side='right' caption='[[1mjc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[1mjc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MJC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MJC 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=1mjc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mjc OCA], [http://pdbe.org/1mjc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mjc RCSB], [http://www.ebi.ac.uk/pdbsum/1mjc PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/CSPA_ECOLI CSPA_ECOLI]] Binds to and stimulates the transcription of the CCAAT-containing, cold-shock-inducible promoters of the H-NS and GyrA proteins. Binds also to the inverted repeat 5'-ATTGG-3'.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mj/1mjc_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

The major cold shock protein of Escherichia coli, CspA, produced upon a rapid downshift in growth temperature, is involved in the transcriptional regulation of at least two genes. The protein shares high homology with the nucleic acid-binding domain of the Y-box factors, a family of eukaryotic proteins involved in transcriptional and translational regulation. The crystal structure of CspA has been determined at 2-A resolution and refined to R = 0.187. CspA is composed of five antiparallel beta-strands forming a closed five-stranded beta-barrel. The three-dimensional structure of CspA is similar to that of the major cold shock protein of Bacillus subtilis, CspB, which has recently been determined at 2.45-A resolution. However, in contrast to CspB, no dimer is formed in the crystal. The surface of CspA is characteristic for a protein interacting with single-stranded nucleic acids. Due to the high homology of the bacterial cold shock proteins with the Y-box factors, E. coli CspA and B. subtilis CspB define a structural framework for the common cold shock domain.

Crystal structure of CspA, the major cold shock protein of Escherichia coli.,Schindelin H, Jiang W, Inouye M, Heinemann U Proc Natl Acad Sci U S A. 1994 May 24;91(11):5119-23. PMID:8197194<ref>PMID:8197194</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Heinemann, U]]

[[Category: Schindelin, H]]

[[Category: Transcription regulation]]