1x2g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1x2g" [edit=sysop:move=sysop])
Current revision (07:42, 23 October 2024) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1x2g.png|left|200px]]
 
-
{{STRUCTURE_1x2g| PDB=1x2g | SCENE= }}
+
==Crystal Structure of Lipate-Protein Ligase A from Escherichia coli==
 +
<StructureSection load='1x2g' size='340' side='right'caption='[[1x2g]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1x2g]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X2G FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1x2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x2g OCA], [https://pdbe.org/1x2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x2g RCSB], [https://www.ebi.ac.uk/pdbsum/1x2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x2g ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/LPLA_ECOLI LPLA_ECOLI] Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to catalyze very poorly the transfer of lipoyl and octanoyl moiety from their acyl carrier protein.<ref>PMID:7639702</ref>
 +
== 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/x2/1x2g_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=1x2g ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Lipoate-protein ligase A (LplA) catalyzes the formation of lipoyl-AMP from lipoate and ATP and then transfers the lipoyl moiety to a specific lysine residue on the acyltransferase subunit of alpha-ketoacid dehydrogenase complexes and on H-protein of the glycine cleavage system. The lypoyllysine arm plays a pivotal role in the complexes by shuttling the reaction intermediate and reducing equivalents between the active sites of the components of the complexes. We have determined the X-ray crystal structures of Escherichia coli LplA alone and in a complex with lipoic acid at 2.4 and 2.9 angstroms resolution, respectively. The structure of LplA consists of a large N-terminal domain and a small C-terminal domain. The structure identifies the substrate binding pocket at the interface between the two domains. Lipoic acid is bound in a hydrophobic cavity in the N-terminal domain through hydrophobic interactions and a weak hydrogen bond between carboxyl group of lipoic acid and the Ser-72 or Arg-140 residue of LplA. No large conformational change was observed in the main chain structure upon the binding of lipoic acid.
-
===Crystal Structure of Lipate-Protein Ligase A from Escherichia coli===
+
Crystal structure of lipoate-protein ligase A from Escherichia coli. Determination of the lipoic acid-binding site.,Fujiwara K, Toma S, Okamura-Ikeda K, Motokawa Y, Nakagawa A, Taniguchi H J Biol Chem. 2005 Sep 30;280(39):33645-51. Epub 2005 Jul 25. PMID:16043486<ref>PMID:16043486</ref>
-
{{ABSTRACT_PUBMED_16043486}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 1x2g" style="background-color:#fffaf0;"></div>
-
[[1x2g]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X2G OCA].
+
== References ==
-
 
+
<references/>
-
==Reference==
+
__TOC__
-
<ref group="xtra">PMID:016043486</ref><references group="xtra"/>
+
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Fujiwara, K.]]
+
[[Category: Large Structures]]
-
[[Category: Motokawa, Y.]]
+
[[Category: Fujiwara K]]
-
[[Category: Nakagawa, A.]]
+
[[Category: Motokawa Y]]
-
[[Category: Okamura-Ikeda, K.]]
+
[[Category: Nakagawa A]]
-
[[Category: Taniguchi, H.]]
+
[[Category: Okamura-Ikeda K]]
-
[[Category: Toma, S.]]
+
[[Category: Taniguchi H]]
-
[[Category: Ligase]]
+
[[Category: Toma S]]
-
[[Category: Lipoate-protein ligase]]
+
-
[[Category: Lipoic acid]]
+
-
[[Category: Post-translational modification]]
+
-
[[Category: Protein acylation]]
+

Current revision

Crystal Structure of Lipate-Protein Ligase A from Escherichia coli

PDB ID 1x2g

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1x2g"
Personal tools