2hsg: Difference between revisions

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{{Seed}}
[[Image:2hsg.png|left|200px]]


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==Structure of transcription regulator CcpA in its DNA-free state==
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<StructureSection load='2hsg' size='340' side='right'caption='[[2hsg]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2hsg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HSG FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hsg OCA], [https://pdbe.org/2hsg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hsg RCSB], [https://www.ebi.ac.uk/pdbsum/2hsg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hsg ProSAT]</span></td></tr>
{{STRUCTURE_2hsg|  PDB=2hsg  |  SCENE= }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/CCPA_PRIMG CCPA_PRIMG] Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hs/2hsg_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2hsg ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The catabolite control protein A (CcpA) from Bacillus megaterium is a member of the bacterial repressor protein family GalR-LacI. CcpA functions as master transcriptional regulator of carbon catabolite repression/regulation in firmicutes. Here we present the crystal structure of full-length apo CcpA at 2.5 A resolution from B. megaterium. The structure reveals the location of the helix-turn-helix domain as well as the hinge region, which were not visible due to their high flexibility in earlier crystallographic studies on CcpA molecules. The structure of the apo CcpA homodimer in the present form is in contrast to other reported structures for CcpA.


===Structure of transcription regulator CcpA in its DNA-free state===
Structure of full-length transcription regulator CcpA in the apo form.,Loll B, Saenger W, Biesiadka J Biochim Biophys Acta. 2007 Jun;1774(6):732-6. Epub 2007 Apr 18. PMID:17500051<ref>PMID:17500051</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2hsg" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_17500051}}, adds the Publication Abstract to the page
*[[Catabolite control protein 3D structures|Catabolite control protein 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 17500051 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_17500051}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
2HSG is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HSG OCA].
[[Category: Priestia megaterium]]
 
[[Category: Alings C]]
==Reference==
[[Category: Biesiadka J]]
<ref group="xtra">PMID:17500051</ref><references group="xtra"/>
[[Category: Loll B]]
[[Category: Bacillus megaterium]]
[[Category: Saenger W]]
[[Category: Alings, C.]]
[[Category: Biesiadka, J.]]
[[Category: Loll, B.]]
[[Category: Saenger, W.]]
[[Category: Ccpa]]
[[Category: Transcriptional regulator]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 17:37:35 2009''

Latest revision as of 13:01, 30 August 2023

Structure of transcription regulator CcpA in its DNA-free stateStructure of transcription regulator CcpA in its DNA-free state

Structural highlights

2hsg is a 1 chain structure with sequence from Priestia megaterium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CCPA_PRIMG Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions.

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 catabolite control protein A (CcpA) from Bacillus megaterium is a member of the bacterial repressor protein family GalR-LacI. CcpA functions as master transcriptional regulator of carbon catabolite repression/regulation in firmicutes. Here we present the crystal structure of full-length apo CcpA at 2.5 A resolution from B. megaterium. The structure reveals the location of the helix-turn-helix domain as well as the hinge region, which were not visible due to their high flexibility in earlier crystallographic studies on CcpA molecules. The structure of the apo CcpA homodimer in the present form is in contrast to other reported structures for CcpA.

Structure of full-length transcription regulator CcpA in the apo form.,Loll B, Saenger W, Biesiadka J Biochim Biophys Acta. 2007 Jun;1774(6):732-6. Epub 2007 Apr 18. PMID:17500051[1]

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

See Also

References

  1. Loll B, Saenger W, Biesiadka J. Structure of full-length transcription regulator CcpA in the apo form. Biochim Biophys Acta. 2007 Jun;1774(6):732-6. Epub 2007 Apr 18. PMID:17500051 doi:10.1016/j.bbapap.2007.03.020

2hsg, resolution 2.50Å

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