4xo1: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

==crystal structure of Se-Met GnsA with double mutations==

== Structural highlights ==

<table><tr><td colspan='2'>[[4xo1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XO1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XO1 FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xo2|4xo2]]</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=4xo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xo1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xo1 RCSB], [http://www.ebi.ac.uk/pdbsum/4xo1 PDBsum]</span></td></tr>

</table>

== Function ==

[[http://www.uniprot.org/uniprot/GNSA_ECOLI GNSA_ECOLI]] Overexpression increases levels of unsaturated fatty acids and suppresses both the temperature-sensitive fabA6 mutation and cold-sensitive secG null mutation.<ref>PMID:11544213</ref>

== Publication Abstract from PubMed ==

Escherichia Coli GnsA is a regulator of phosphatidylethanolamine synthesis and functions as a suppressor of both a secG null mutation and fabA6 mutations. GnsA may also be a toxin with the cognate antitoxin YmcE. Here we report the crystal structure of GnsA to 1.8 A. GnsA forms a V shaped hairpin structure that is tightly associated into a homodimer. Our comprehensive structural study suggests that GnsA is structurally similar to an outer membrane protein, suggesting a function of protein binding.

~~The entry 4xo1 is ON HOLD until Paper Publication~~

Crystal structure of GnsA from Escherichia coli.,Wei Y, Zhan L, Gao Z, Prive GG, Dong Y Biochem Biophys Res Commun. 2015 Jun 19;462(1):1-7. doi:, 10.1016/j.bbrc.2015.03.133. Epub 2015 Apr 1. PMID:25839658<ref>PMID:25839658</ref>

~~Authors: Zhan~~, L.H.~~, Gao, Z.Q., Dong, Y.H~~.

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

</div>

~~Description: crystal structure of Se-Met GnsA with double mutations~~

== References ==

[[Category: ~~Unreleased Structures~~]]

[[Category: Gao, Z.Q]]

__TOC__

[[Category: Zhan, L.H]]

</StructureSection>

[[Category: ~~Dong, Y.H~~]]

[[Category: Dong, Y]]

[[Category: Gao, Z]]

[[Category: Zhan, L]]

[[Category: Protein binding]]

[[Category: Suppressor]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==crystal structure of Se-Met GnsA with double mutations==
+<StructureSection load='4xo1' size='340' side='right' caption='[[4xo1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4xo1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XO1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XO1 FirstGlance]. <br>
+</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xo2|4xo2]]</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=4xo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xo1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xo1 RCSB], [http://www.ebi.ac.uk/pdbsum/4xo1 PDBsum]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/GNSA_ECOLI GNSA_ECOLI]] Overexpression increases levels of unsaturated fatty acids and suppresses both the temperature-sensitive fabA6 mutation and cold-sensitive secG null mutation.<ref>PMID:11544213</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Escherichia Coli GnsA is a regulator of phosphatidylethanolamine synthesis and functions as a suppressor of both a secG null mutation and fabA6 mutations. GnsA may also be a toxin with the cognate antitoxin YmcE. Here we report the crystal structure of GnsA to 1.8 A. GnsA forms a V shaped hairpin structure that is tightly associated into a homodimer. Our comprehensive structural study suggests that GnsA is structurally similar to an outer membrane protein, suggesting a function of protein binding.
-The entry 4xo1 is ON HOLD  until Paper Publication
+Crystal structure of GnsA from Escherichia coli.,Wei Y, Zhan L, Gao Z, Prive GG, Dong Y Biochem Biophys Res Commun. 2015 Jun 19;462(1):1-7. doi:, 10.1016/j.bbrc.2015.03.133. Epub 2015 Apr 1. PMID:25839658<ref>PMID:25839658</ref>
-Authors: Zhan, L.H., Gao, Z.Q., Dong, Y.H.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: crystal structure of Se-Met GnsA with double mutations
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
-[[Category: Gao, Z.Q]]
+__TOC__
-[[Category: Zhan, L.H]]
+</StructureSection>
-[[Category: Dong, Y.H]]
+[[Category: Dong, Y]]
+[[Category: Gao, Z]]
+[[Category: Zhan, L]]
+[[Category: Protein binding]]
+[[Category: Suppressor]]