1kng: Difference between revisions

Line 1:

~~{{STRUCTURE_1kng| PDB=1kng | SCENE= }}~~

==Crystal structure of CcmG reducing oxidoreductase at 1.14 A==

===Crystal structure of CcmG reducing oxidoreductase at 1.14 A===

~~{{ABSTRACT_PUBMED_12121652}}~~

== Structural highlights ==

<table><tr><td colspan='2'>[[1kng]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bradyrhizobium_japonicum Bradyrhizobium japonicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KNG FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cycy ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=375 Bradyrhizobium japonicum])</td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kng OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kng RCSB], [http://www.ebi.ac.uk/pdbsum/1kng PDBsum]</span></td></tr>

<table>

== Evolutionary Conservation ==

[[Image:Consurf_key_small.gif|200px|right]]

Check<jmol>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kn/1kng_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/chain_selection.php?pdb_ID=2ata ConSurf].

== Publication Abstract from PubMed ==

CcmG is unlike other periplasmic thioredoxin (TRX)-like proteins in that it has a specific reducing activity in an oxidizing environment and a high fidelity of interaction. These two unusual properties are required for its role in c-type cytochrome maturation. The crystal structure of CcmG reveals a modified TRX fold with an unusually acidic active site and a groove formed from two inserts in the fold. Deletion of one of the groove-forming inserts disrupts c-type cytochrome formation. Two unique structural features of CcmG-an acidic active site and an adjacent groove-appear to be necessary to convert an indiscriminately binding scaffold, the TRX fold, into a highly specific redox protein.

~~==Function==~~

Structure of CcmG/DsbE at 1.14 A resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment.,Edeling MA, Guddat LW, Fabianek RA, Thony-Meyer L, Martin JL Structure. 2002 Jul;10(7):973-9. PMID:12121652<ref>PMID:12121652</ref>

~~[[http:/~~/~~www~~.~~uniprot.org/uniprot/CYCY_BRAJA CYCY_BRAJA]] Required for disulfide bond formation~~ in ~~some periplasmic proteins~~. ~~Also act as a disulfide oxidoreductase in cytochromes c biogenesis~~. ~~The cysteines of apocytochromes c must be in the reduced state for covalent linkage between the two moieties to occur~~ (~~By similarity~~).

~~==About this Structure==~~

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

~~[[1kng]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Bradyrhizobium_japonicum Bradyrhizobium japonicum]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1KNG OCA].~~

</div>

== References ==

==~~Reference~~==

~~<ref group="xtra">PMID:012121652</ref>~~<references ~~group="xtra"~~/><~~references~~/>

__TOC__

</StructureSection>

[[Category: Bradyrhizobium japonicum]]

[[Category: Edeling, M A.]]

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@@ Line 1: / Line 1: @@
-{{STRUCTURE_1kng|  PDB=1kng  |  SCENE=  }}
+==Crystal structure of CcmG reducing oxidoreductase at 1.14 A==
-===Crystal structure of CcmG reducing oxidoreductase at 1.14 A===
+<StructureSection load='1kng' size='340' side='right' caption='[[1kng]], [[Resolution|resolution]] 1.14&Aring;' scene=''>
-{{ABSTRACT_PUBMED_12121652}}
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1kng]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bradyrhizobium_japonicum Bradyrhizobium japonicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KNG FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cycy ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=375 Bradyrhizobium japonicum])</td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kng OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kng RCSB], [http://www.ebi.ac.uk/pdbsum/1kng PDBsum]</span></td></tr>
+<table>
+== 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/kn/1kng_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/chain_selection.php?pdb_ID=2ata ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+CcmG is unlike other periplasmic thioredoxin (TRX)-like proteins in that it has a specific reducing activity in an oxidizing environment and a high fidelity of interaction. These two unusual properties are required for its role in c-type cytochrome maturation. The crystal structure of CcmG reveals a modified TRX fold with an unusually acidic active site and a groove formed from two inserts in the fold. Deletion of one of the groove-forming inserts disrupts c-type cytochrome formation. Two unique structural features of CcmG-an acidic active site and an adjacent groove-appear to be necessary to convert an indiscriminately binding scaffold, the TRX fold, into a highly specific redox protein.
-==Function==
+Structure of CcmG/DsbE at 1.14 A resolution: high-fidelity reducing activity in an indiscriminately oxidizing environment.,Edeling MA, Guddat LW, Fabianek RA, Thony-Meyer L, Martin JL Structure. 2002 Jul;10(7):973-9. PMID:12121652<ref>PMID:12121652</ref>
-[[http://www.uniprot.org/uniprot/CYCY_BRAJA CYCY_BRAJA]] Required for disulfide bond formation in some periplasmic proteins. Also act as a disulfide oxidoreductase in cytochromes c biogenesis. The cysteines of apocytochromes c must be in the reduced state for covalent linkage between the two moieties to occur (By similarity).
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[1kng]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bradyrhizobium_japonicum Bradyrhizobium japonicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KNG OCA].
+</div>
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:012121652</ref><references group="xtra"/><references/>
+__TOC__
+</StructureSection>
 [[Category: Bradyrhizobium japonicum]]
 [[Category: Edeling, M A.]]