4cf7: Difference between revisions

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<StructureSection load='4cf7' size='340' side='right'caption='[[4cf7]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
<StructureSection load='4cf7' size='340' side='right'caption='[[4cf7]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4cf7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CF7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CF7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4cf7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CF7 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] </span></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=4cf7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cf7 OCA], [https://pdbe.org/4cf7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cf7 RCSB], [https://www.ebi.ac.uk/pdbsum/4cf7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cf7 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=4cf7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cf7 OCA], [http://pdbe.org/4cf7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cf7 RCSB], [http://www.ebi.ac.uk/pdbsum/4cf7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cf7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/KAD_AQUAE KAD_AQUAE]] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in the energy metabolism and nucleotide synthesis, is essential for maintenance and cell growth (By similarity).  
[[https://www.uniprot.org/uniprot/KAD_AQUAE KAD_AQUAE]] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in the energy metabolism and nucleotide synthesis, is essential for maintenance and cell growth (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Kinases perform phosphoryl-transfer reactions in milliseconds; without enzymes, these reactions would take about 8,000 years under physiological conditions. Despite extensive studies, a comprehensive understanding of kinase energy landscapes, including both chemical and conformational steps, is lacking. Here we scrutinize the microscopic steps in the catalytic cycle of adenylate kinase, through a combination of NMR measurements during catalysis, pre-steady-state kinetics, molecular-dynamics simulations and crystallography of active complexes. We find that the Mg2+ cofactor activates two distinct molecular events: phosphoryl transfer (&gt;105-fold) and lid opening (103-fold). In contrast, mutation of an essential active site arginine decelerates phosphoryl transfer 103-fold without substantially affecting lid opening. Our results highlight the importance of the entire energy landscape in catalysis and suggest that adenylate kinases have evolved to activate key processes simultaneously by precise placement of a single, charged and very abundant cofactor in a preorganized active site.
 
The energy landscape of adenylate kinase during catalysis.,Kerns SJ, Agafonov RV, Cho YJ, Pontiggia F, Otten R, Pachov DV, Kutter S, Phung LA, Murphy PN, Thai V, Alber T, Hagan MF, Kern D Nat Struct Mol Biol. 2015 Jan 12. doi: 10.1038/nsmb.2941. PMID:25580578<ref>PMID:25580578</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4cf7" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]]
*[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aquifex aeolicus huber and stetter 2001]]
[[Category: Aquifex aeolicus]]
[[Category: Adenylate kinase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Agafonov, R V]]
[[Category: Agafonov RV]]
[[Category: Cho, Y J]]
[[Category: Cho Y-J]]
[[Category: Hagan, M F]]
[[Category: Hagan MF]]
[[Category: Kern, D]]
[[Category: Kern D]]
[[Category: Kerns, S J]]
[[Category: Kerns SJ]]
[[Category: Kutter, S]]
[[Category: Kutter S]]
[[Category: Murphy, P N]]
[[Category: Murphy PN]]
[[Category: Otten, R]]
[[Category: Otten R]]
[[Category: Pachov, D V]]
[[Category: Pachov DV]]
[[Category: Phung, L A]]
[[Category: Phung LA]]
[[Category: Pontiggia, F]]
[[Category: Pontiggia F]]
[[Category: Thai, V]]
[[Category: Thai V]]
[[Category: Nucleotide-binding]]
[[Category: Phosphoryl transfer]]
[[Category: Transferase]]

Revision as of 20:42, 7 September 2022

Crystal structure of adenylate kinase from Aquifex aeolicus with MgADP boundCrystal structure of adenylate kinase from Aquifex aeolicus with MgADP bound

Structural highlights

4cf7 is a 2 chain structure with sequence from Aquifex aeolicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KAD_AQUAE] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in the energy metabolism and nucleotide synthesis, is essential for maintenance and cell growth (By similarity).

See Also

4cf7, resolution 1.59Å

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OCA
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