3r07

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
 +
==Structural analysis of an archaeal lipoylation system. A bi-partite lipoate protein ligase and its E2 lipoyl domain from Thermoplasma acidophilum==
==Structural analysis of an archaeal lipoylation system. A bi-partite lipoate protein ligase and its E2 lipoyl domain from Thermoplasma acidophilum==
<StructureSection load='3r07' size='340' side='right' caption='[[3r07]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='3r07' size='340' side='right' caption='[[3r07]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3r07]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum_dsm_1728 Thermoplasma acidophilum dsm 1728]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R07 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R07 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3r07]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Theac Theac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R07 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R07 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lplA, Ta0514 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273075 Thermoplasma acidophilum DSM 1728]), Ta0513, Ta0513m ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273075 Thermoplasma acidophilum DSM 1728])</td></tr>
+
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lplA, Ta0514 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273075 THEAC]), Ta0513, Ta0513m ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273075 THEAC])</td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lipoate--protein_ligase Lipoate--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.63 2.7.7.63] </span></td></tr>
+
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.63 2.7.7.63] </span></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=3r07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r07 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r07 RCSB], [http://www.ebi.ac.uk/pdbsum/3r07 PDBsum]</span></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=3r07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r07 OCA], [http://pdbe.org/3r07 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3r07 RCSB], [http://www.ebi.ac.uk/pdbsum/3r07 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3r07 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/LPLA_THEAC LPLA_THEAC]] Part of a lipoate-protein ligase complex that 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. Can also use octanoate as substrate.<ref>PMID:16384580</ref> <ref>PMID:19594830</ref> <ref>PMID:19520844</ref> <ref>PMID:16141198</ref> [[http://www.uniprot.org/uniprot/LPLAC_THEAC LPLAC_THEAC]] Part of a lipoate-protein ligase complex that 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. Can also use octanoate as substrate.<ref>PMID:16384580</ref> <ref>PMID:19594830</ref> <ref>PMID:19520844</ref>
+
[[http://www.uniprot.org/uniprot/LPLAN_THEAC LPLAN_THEAC]] Part of a lipoate-protein ligase complex that 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. Can also use octanoate as substrate.<ref>PMID:16141198</ref> <ref>PMID:19520844</ref> <ref>PMID:19594830</ref> [[http://www.uniprot.org/uniprot/LPLAC_THEAC LPLAC_THEAC]] Part of a lipoate-protein ligase complex that 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. Can also use octanoate as substrate.<ref>PMID:16384580</ref> <ref>PMID:19594830</ref> <ref>PMID:19520844</ref>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Lipoate--protein ligase]]
+
[[Category: Theac]]
-
[[Category: Thermoplasma acidophilum dsm 1728]]
+
[[Category: Transferase]]
[[Category: Crennell, S]]
[[Category: Crennell, S]]
[[Category: Posner, M G]]
[[Category: Posner, M G]]
Line 23: Line 24:
[[Category: Bi-partite]]
[[Category: Bi-partite]]
[[Category: Ligase]]
[[Category: Ligase]]
-
[[Category: Transferase]]
 

Revision as of 21:29, 4 August 2016

Structural analysis of an archaeal lipoylation system. A bi-partite lipoate protein ligase and its E2 lipoyl domain from Thermoplasma acidophilum

3r07, resolution 2.70Å

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/3r07"
Personal tools