View source for 4x8m


==Crystal structure of E. coli Adenylate kinase Y171W mutant==
<StructureSection load='4x8m' size='340' side='right'caption='[[4x8m]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4x8m]] is a 1 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=4X8M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X8M 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]] 2.6&#8491;</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=4x8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x8m OCA], [https://pdbe.org/4x8m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x8m RCSB], [https://www.ebi.ac.uk/pdbsum/4x8m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x8m ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KAD_ECOLI KAD_ECOLI] 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.[HAMAP-Rule:MF_00235]
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== Publication Abstract from PubMed ==
An emerging paradigm in enzymology is that transient high-energy structural states play crucial roles in enzymatic reaction cycles. Generally, these high-energy or 'invisible' states cannot be studied directly at atomic resolution using existing structural and spectroscopic techniques owing to their low populations or short residence times. Here we report the direct NMR-based detection of the molecular topology and conformational dynamics of a catalytically indispensable high-energy state of an adenylate kinase variant. On the basis of matching energy barriers for conformational dynamics and catalytic turnover, it was found that the enzyme's catalytic activity is governed by its dynamic interconversion between the high-energy state and a ground state structure that was determined by X-ray crystallography. Our results show that it is possible to rationally tune enzymes' conformational dynamics and hence their catalytic power-a key aspect in rational design of enzymes catalysing novel reactions.

Structural basis for catalytically restrictive dynamics of a high-energy enzyme state.,Kovermann M, Aden J, Grundstrom C, Elisabeth Sauer-Eriksson A, Sauer UH, Wolf-Watz M Nat Commun. 2015 Jul 3;6:7644. doi: 10.1038/ncomms8644. PMID:26138143<ref>PMID:26138143</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4x8m" style="background-color:#fffaf0;"></div>

==See Also==
*[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Aden J]]
[[Category: Grundstrom C]]
[[Category: Kovermann M]]
[[Category: Sauer UH]]
[[Category: Sauer-Eriksson AE]]
[[Category: Wolf-Watz M]]