1sr3: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
New page: left|200px<br /><applet load="1sr3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sr3" /> '''Solution structure of the heme chaperone Ccm...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(15 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1sr3.gif|left|200px]]<br /><applet load="1sr3" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1sr3" />
'''Solution structure of the heme chaperone CcmE of Escherichia coli'''<br />


==Overview==
==Solution structure of the heme chaperone CcmE of Escherichia coli==
The concept of metal chaperones involves transient binding of metallic, cofactors by specific proteins for delivery to enzymes in which they, function. Metal chaperones thus provide a protective, as well as a, transport, function. We report the first structure of a heme chaperone, CcmE, which comprises these two functions. We propose that the covalent, attachment of heme to an exposed histidine occurs after heme binding at, the surface of a rigid molecule with a flexible C-terminal domain. CcmE, belongs to a family of proteins with a specific fold, which all share a, function in delivery of specific molecular cargo.
<StructureSection load='1sr3' size='340' side='right'caption='[[1sr3]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1sr3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1liz 1liz]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SR3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SR3 FirstGlance]. <br>
</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=1sr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sr3 OCA], [https://pdbe.org/1sr3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sr3 RCSB], [https://www.ebi.ac.uk/pdbsum/1sr3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sr3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CCME_ECOLI CCME_ECOLI] Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.[HAMAP-Rule:MF_01959]
== 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/sr/1sr3_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=1sr3 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The concept of metal chaperones involves transient binding of metallic cofactors by specific proteins for delivery to enzymes in which they function. Metal chaperones thus provide a protective, as well as a transport, function. We report the first structure of a heme chaperone, CcmE, which comprises these two functions. We propose that the covalent attachment of heme to an exposed histidine occurs after heme binding at the surface of a rigid molecule with a flexible C-terminal domain. CcmE belongs to a family of proteins with a specific fold, which all share a function in delivery of specific molecular cargo.


==About this Structure==
NMR structure of the heme chaperone CcmE reveals a novel functional motif.,Enggist E, Thony-Meyer L, Guntert P, Pervushin K Structure. 2002 Nov;10(11):1551-7. PMID:12429096<ref>PMID:12429096</ref>
1SR3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure superseeds the now removed PDB entry 1LIZ. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SR3 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
NMR structure of the heme chaperone CcmE reveals a novel functional motif., Enggist E, Thony-Meyer L, Guntert P, Pervushin K, Structure. 2002 Nov;10(11):1551-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12429096 12429096]
</div>
<div class="pdbe-citations 1sr3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Enggist, E.]]
[[Category: Enggist E]]
[[Category: Guntert, P.]]
[[Category: Guntert P]]
[[Category: Pervushin, K.]]
[[Category: Pervushin K]]
[[Category: Thony-Meyer, L.]]
[[Category: Thony-Meyer L]]
[[Category: beta barrel]]
[[Category: flexible c-terminal domain]]
[[Category: ob fold]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:35:30 2007''
Retrieved from "https://proteopedia.org/1sr3"