1ank

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[[Image:1ank.gif|left|200px]]
 
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{{Structure
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==THE CLOSED CONFORMATION OF A HIGHLY FLEXIBLE PROTEIN: THE STRUCTURE OF E. COLI ADENYLATE KINASE WITH BOUND AMP AND AMPPNP==
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|PDB= 1ank |SIZE=350|CAPTION= <scene name='initialview01'>1ank</scene>, resolution 2.0&Aring;
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<StructureSection load='1ank' size='340' side='right'caption='[[1ank]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene> and <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'>ANP</scene>
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<table><tr><td colspan='2'>[[1ank]] 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=1ANK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ANK FirstGlance]. <br>
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|ACTIVITY= [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]
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</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&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ank FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ank OCA], [https://pdbe.org/1ank PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ank RCSB], [https://www.ebi.ac.uk/pdbsum/1ank PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ank ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/an/1ank_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ank ConSurf].
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<div style="clear:both"></div>
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'''THE CLOSED CONFORMATION OF A HIGHLY FLEXIBLE PROTEIN: THE STRUCTURE OF E. CLOI ADENYLATE KINASE WITH BOUND AMP AND AMPPNP'''
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==See Also==
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*[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The structure of E. coli adenylate kinase with bound AMP and AMPPNP at 2.0 A resolution is presented. The protein crystallizes in space group C2 with two molecules in the asymmetric unit, and has been refined to an R factor of 20.1% and an Rfree of 31.6%. In the present structure, the protein is in the closed (globular) form with the large flexible lid domain covering the AMPPNP molecule. Within the protein, AMP and AMPPNP, and ATP analog, occupy the AMP and ATP sites respectively, which had been suggested by the most recent crystal structure of E. coli adenylate kinase with Ap5A bound (Muller and Schulz, 1992, ref. 1) and prior fluorescence studies (Liang et al., 1991, ref. 2). The binding of substrates and the positions of the active site residues are compared between the present structure and the E. coli adenylate kinase/Ap5A structure. We failed to detect a peak in the density map corresponding to the Mg2+ ion which is required for catalysis, and its absence has been attributed to the use of ammonium sulfate in the crystallization solution. Finally, a comparison is made between the present structure and the structure of the heavy chain of muscle myosin.
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==About this Structure==
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1ANK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ANK OCA].
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==Reference==
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The closed conformation of a highly flexible protein: the structure of E. coli adenylate kinase with bound AMP and AMPPNP., Berry MB, Meador B, Bilderback T, Liang P, Glaser M, Phillips GN Jr, Proteins. 1994 Jul;19(3):183-98. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7937733 7937733]
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[[Category: Adenylate kinase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Berry, M B.]]
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[[Category: Berry MB]]
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[[Category: Bilderback, T.]]
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[[Category: Bilderback T]]
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[[Category: Glaser, M.]]
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[[Category: Glaser M]]
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[[Category: Jr., G N.Phillips.]]
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[[Category: Liang P]]
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[[Category: Liang, P.]]
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[[Category: Meador B]]
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[[Category: Meador, B.]]
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[[Category: Phillips Jr GN]]
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[[Category: AMP]]
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[[Category: ANP]]
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[[Category: transferase(phosphotransferase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:59:57 2008''
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Current revision

THE CLOSED CONFORMATION OF A HIGHLY FLEXIBLE PROTEIN: THE STRUCTURE OF E. COLI ADENYLATE KINASE WITH BOUND AMP AND AMPPNP

PDB ID 1ank

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