3kh9: Difference between revisions

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[[Image:3kh9.png|left|200px]]


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==Crystal structure of the periplasmic soluble domain of oxidized CcmG from Pseudomonas aeruginosa==
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<StructureSection load='3kh9' size='340' side='right'caption='[[3kh9]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3kh9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KH9 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]] 2.2&#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=3kh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kh9 OCA], [https://pdbe.org/3kh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kh9 RCSB], [https://www.ebi.ac.uk/pdbsum/3kh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kh9 ProSAT]</span></td></tr>
{{STRUCTURE_3kh9|  PDB=3kh9  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/DSBE_PSEAE DSBE_PSEAE] Involved in disulfide bond formation. Catalyzes a late, reductive step in the assembly of periplasmic c-type cytochromes, probably the reduction of disulfide bonds of the apocytochrome c to allow covalent linkage with the heme. Possible subunit of a heme lyase (By similarity).
== 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/kh/3kh9_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3kh9 ConSurf].
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== Publication Abstract from PubMed ==
The cytochrome c maturation process is carried out in the bacterial periplasm, where some specialized thiol-disulfide oxidoreductases work in close synergy for the correct reduction of oxidized apocytochrome before covalent heme attachment. We present a structural and functional characterization of the soluble periplasmic domain of CcmG from the opportunistic pathogen P. aeruginosa (Pa-CcmG), a component of the protein machinery involved in cyt c maturation in gram-negative bacteria. X-ray crystallography reveals that Pa-CcmG is a TRX-like protein; high-resolution crystal structures show that the oxidized and the reduced forms of the enzyme are identical except for the active-site disulfide. The standard redox potential was calculated to be E(0') = -0.213 V at pH 7.0; the pK(a) of the active site thiols were pK(a) = 6.13 +/- 0.05 for the N-terminal Cys74 and pK(a) = 10.5 +/- 0.17 for the C-terminal Cys77. Experiments were carried out to characterize and isolate the mixed disulfide complex between Pa-CcmG and Pa-CcmH (the other redox active component of System I in P. aeruginosa). Our data indicate that the target disulfide of this TRX-like protein is not the intramolecular disulfide of oxidized Pa-CcmH, but the intermolecular disulfide formed between Cys28 of Pa-CcmH and DTNB used for the in vitro experiments. This observation suggests that, in vivo, the physiological substrate of Pa-CcmG may be the mixed-disulfide complex between Pa-CcmH and apo-cyt.


===Crystal structure of the periplasmic soluble domain of oxidized CcmG from Pseudomonas aeruginosa===
Structural and functional characterization of CcmG from Pseudomonas aeruginosa, a key component of the bacterial cytochrome c maturation apparatus.,Di Matteo A, Calosci N, Gianni S, Jemth P, Brunori M, Travaglini-Allocatelli C Proteins. 2010 Aug 1;78(10):2213-21. PMID:20544959<ref>PMID:20544959</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3kh9" style="background-color:#fffaf0;"></div>


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==See Also==
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*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 20544959 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_20544959}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
3KH9 is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KH9 OCA].
 
==Reference==
<ref group="xtra">PMID:20544959</ref><references group="xtra"/>
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Allocatelli, C Travaglini.]]
[[Category: Brunori M]]
[[Category: Brunori, M.]]
[[Category: Calosci N]]
[[Category: Calosci, N.]]
[[Category: Di Matteo A]]
[[Category: Gianni, S.]]
[[Category: Gianni S]]
[[Category: Jemth, P.]]
[[Category: Jemth P]]
[[Category: Matteo, A Di.]]
[[Category: Travaglini Allocatelli C]]
[[Category: Cell inner membrane]]
[[Category: Cytochrome c-type biogenesis]]
[[Category: Disulfide bond]]
[[Category: Oxidoreductase]]
[[Category: Redox-active center]]
[[Category: Thiol-disulfide exchange]]
[[Category: Transmembrane]]
[[Category: Trx-like]]
 
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