We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1qjc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:46, 13 December 2023) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1qjc.gif|left|200px]]<br /><applet load="1qjc" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1qjc, resolution 1.63&Aring;" />
 
-
'''PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE IN COMPLEX WITH AMPCPP AND 4'-PHOSPHOPANTETHEINE FROM ESCHERICHIA COLI'''<br />
 
-
==Overview==
+
==Phosphopantetheine Adenylyltransferase from Escherichia coli in complex with 4'-phosphopantetheine==
-
Phosphopantetheine adenylyltransferase (PPAT) is an essential enzyme in, the coenzyme A pathway that catalyzes the reversible transfer of an, adenylyl group from ATP to 4'-phosphopantetheine (Ppant) in the presence, of magnesium. To investigate the reaction mechanism, the high-resolution, crystal structures of the Escherichia coli PPAT have been determined in, the presence of either ATP or Ppant. Structural details of the catalytic, center revealed specific roles for individual amino acid residues involved, in substrate binding and catalysis. The side-chain of His18 stabilizes the, expected pentacovalent intermediate, whereas the side-chains of Thr10 and, Lys42 orient the nucleophile for an in-line displacement mechanism. The, binding site for the manganese ion that interacts with the phosphate, groups of the nucleotide has also been identified. Within the PPAT, hexamer, one trimer is in its substrate-free state, whereas the other is, in a substrate-bound state.
+
<StructureSection load='1qjc' size='340' side='right'caption='[[1qjc]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1qjc]] is a 2 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=1QJC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QJC 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]] 1.63&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1qjc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qjc OCA], [https://pdbe.org/1qjc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qjc RCSB], [https://www.ebi.ac.uk/pdbsum/1qjc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qjc ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/COAD_ECOLI COAD_ECOLI] Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
 +
== 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/qj/1qjc_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/main_output.php?pdb_ID=1qjc ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Phosphopantetheine adenylyltransferase (PPAT) is an essential enzyme in the coenzyme A pathway that catalyzes the reversible transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) in the presence of magnesium. To investigate the reaction mechanism, the high-resolution crystal structures of the Escherichia coli PPAT have been determined in the presence of either ATP or Ppant. Structural details of the catalytic center revealed specific roles for individual amino acid residues involved in substrate binding and catalysis. The side-chain of His18 stabilizes the expected pentacovalent intermediate, whereas the side-chains of Thr10 and Lys42 orient the nucleophile for an in-line displacement mechanism. The binding site for the manganese ion that interacts with the phosphate groups of the nucleotide has also been identified. Within the PPAT hexamer, one trimer is in its substrate-free state, whereas the other is in a substrate-bound state.
-
==About this Structure==
+
The crystal structures of phosphopantetheine adenylyltransferase with bound substrates reveal the enzyme's catalytic mechanism.,Izard T J Mol Biol. 2002 Jan 25;315(4):487-95. PMID:11812124<ref>PMID:11812124</ref>
-
1QJC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and PNS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pantetheine-phosphate_adenylyltransferase Pantetheine-phosphate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.3 2.7.7.3] Known structural/functional Site: <scene name='pdbsite=ACT:Pns Binding Site For Chain B'>ACT</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QJC OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
The crystal structures of phosphopantetheine adenylyltransferase with bound substrates reveal the enzyme's catalytic mechanism., Izard T, J Mol Biol. 2002 Jan 25;315(4):487-95. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11812124 11812124]
+
</div>
 +
<div class="pdbe-citations 1qjc" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Pantetheine-phosphate adenylyltransferase]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Izard T]]
-
[[Category: Izard, T.]]
+
-
[[Category: PNS]]
+
-
[[Category: SO4]]
+
-
[[Category: coenzyme a biosynthesis]]
+
-
[[Category: nucleotidyltransferase]]
+
-
[[Category: transferase]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:53:46 2007''
+

Current revision

Phosphopantetheine Adenylyltransferase from Escherichia coli in complex with 4'-phosphopantetheine

PDB ID 1qjc

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/1qjc"
Personal tools