3kta

From Proteopedia

(Difference between revisions)

Current revision

Structural Basis for Adenylate Kinase Activity in ABC ATPases

Structural highlights

3kta is a 4 chain structure with sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.627Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SMC_PYRFU Required for chromosome condensation and partitioning (By similarity). Binds single-stranded but not double-stranded DNA.[HAMAP-Rule:MF_01894]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

ATP-binding cassette (ABC) enzymes are involved in diverse biological processes ranging from transmembrane transport to chromosome cohesion and DNA repair. They typically use ATP hydrolysis to conduct energy-dependent biological reactions. However, the cystic fibrosis transmembrane conductance regulator and the DNA repair protein Rad50 can also catalyze the adenylate kinase reaction (ATP+AMP<-->2ADP). To clarify and provide a mechanistic basis for the adenylate kinase activity of ABC enzymes, we report the crystal structure of the nucleotide-binding domain of the Pyrococcus furiosus structural maintenance of chromosome protein (pfSMC(nbd)) in complex with the adenylate kinase inhibitor P(1),P(5)-di(adenosine-5')pentaphosphate. We show that pfSMC(nbd) possesses reverse adenylate kinase activity. Our results suggest that in adenylate kinase reactions, ATP binds to its canonical binding site while AMP binds to the Q-loop glutamine and a hydration water of the Mg(2+) ion. Furthermore, mutational analysis indicates that adenylate kinase reaction occurs in the engaged pfSMC(nbd) dimer and requires the Signature motif for phosphate transfer. Our results explain how ATP hydrolysis and adenylate kinase reactions can be catalyzed by the same functional motifs within the structural framework of ABC enzymes. Thus, adenylate kinase activity is likely to be a latent activity in many ABC enzymes.

Structural basis for adenylate kinase activity in ABC ATPases.,Lammens A, Hopfner KP J Mol Biol. 2010 Aug 13;401(2):265-73. Epub 2010 Jun 19. PMID:20600125^[1]

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

References

↑ Lammens A, Hopfner KP. Structural basis for adenylate kinase activity in ABC ATPases. J Mol Biol. 2010 Aug 13;401(2):265-73. Epub 2010 Jun 19. PMID:20600125 doi:10.1016/j.jmb.2010.06.029

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3kta"

Categories: Large Structures | Pyrococcus furiosus | Hopfner KP | Lammens A

@@ Line 3: / Line 3: @@
 <StructureSection load='3kta' size='340' side='right'caption='[[3kta]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3kta]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KTA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KTA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3kta]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KTA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KTA FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AP5:BIS(ADENOSINE)-5-PENTAPHOSPHATE'>AP5</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.627&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AP5:BIS(ADENOSINE)-5-PENTAPHOSPHATE'>AP5</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PF1843 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 ATCC 43587])</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=3kta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kta OCA], [https://pdbe.org/3kta PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kta RCSB], [https://www.ebi.ac.uk/pdbsum/3kta PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kta ProSAT]</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=3kta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kta OCA], [http://pdbe.org/3kta PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kta RCSB], [http://www.ebi.ac.uk/pdbsum/3kta PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kta ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SMC_PYRFU SMC_PYRFU]] Required for chromosome condensation and partitioning (By similarity). Binds single-stranded but not double-stranded DNA.[HAMAP-Rule:MF_01894]
+[https://www.uniprot.org/uniprot/SMC_PYRFU SMC_PYRFU] Required for chromosome condensation and partitioning (By similarity). Binds single-stranded but not double-stranded DNA.[HAMAP-Rule:MF_01894]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 16: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kt/3kta_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 34: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 43587]]
 [[Category: Large Structures]]
-[[Category: Hopfner, K P]]
+[[Category: Pyrococcus furiosus]]
-[[Category: Lammens, A]]
+[[Category: Hopfner KP]]
-[[Category: Abc atpase]]
+[[Category: Lammens A]]
-[[Category: Adenylate kinase]]
-[[Category: Ap5a]]
-[[Category: Cftr]]
-[[Category: Smc]]
-[[Category: Structural maintenance of chromosome]]
-[[Category: Transferase]]

3kta

From Proteopedia

Current revision

Structural Basis for Adenylate Kinase Activity in ABC ATPases

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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