View source for 6hap


==Adenylate kinase==
<StructureSection load='6hap' size='340' side='right'caption='[[6hap]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6hap]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HAP 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></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6hma|6hma]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6hap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hap OCA], [http://pdbe.org/6hap PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hap RCSB], [http://www.ebi.ac.uk/pdbsum/6hap PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hap ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/KAD_ECO24 KAD_ECO24]] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.[HAMAP-Rule:MF_00235] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Folding of proteins to their functional conformation is paramount to life. Though 75% of the proteome consists of multidomain proteins, our knowledge of folding has been based primarily on studies conducted on single-domain and fast-folding proteins. Nonetheless, the complexity of folding landscapes exhibited by multidomain proteins has received increased scrutiny in recent years. We study the three-domain protein adenylate kinase from E. coli (AK), which has been shown to fold through a series of pathways involving several intermediate states. We use a protein design method to manipulate the folding landscape of AK, and single-molecule FRET spectroscopy to study the effects on the folding process. Mutations introduced in the NMP binding (NMPbind) domain of the protein are found to have unexpected effects on the folding landscape. Thus, while stabilizing mutations in the core of the NMPbind domain retain the main folding pathways of wild-type AK, a destabilizing mutation at the interface between the NMPbind and the CORE domains causes a significant repartition of the flux between the folding pathways. Our results demonstrate the outstanding plasticity of the folding landscape of AK and reveal how specific mutations in the primary structure are translated into changes in folding dynamics. The combination of methodologies introduced in this work should prove useful for deepening our understanding of the folding process of multidomain proteins.

Manipulating the Folding Landscape of a Multidomain Protein.,Kantaev R, Riven I, Goldenzweig A, Barak Y, Dym O, Peleg Y, Albeck S, Fleishman SJ, Haran G J Phys Chem B. 2018 Dec 13;122(49):11030-11038. doi: 10.1021/acs.jpcb.8b04834., Epub 2018 Aug 23. PMID:30088929<ref>PMID:30088929</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6hap" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Adenylate kinase]]
[[Category: Large Structures]]
[[Category: Albek, S]]
[[Category: Barak, Y]]
[[Category: Dym, O]]
[[Category: Fleishman, S J]]
[[Category: Goldenzweig, A]]
[[Category: Haran, G]]
[[Category: Inbal, R]]
[[Category: Kantaev, R]]
[[Category: Peleg, Y]]
[[Category: Adenylat kinase]]
[[Category: Transferase]]