1ak2
From Proteopedia
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(New page: 200px<br /><applet load="1ak2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ak2, resolution 1.92Å" /> '''ADENYLATE KINASE ISO...) |
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| - | [[Image:1ak2.gif|left|200px]]<br /><applet load="1ak2" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1ak2, resolution 1.92Å" /> | ||
| - | '''ADENYLATE KINASE ISOENZYME-2'''<br /> | ||
| - | == | + | ==ADENYLATE KINASE ISOENZYME-2== |
| - | In vertebrates, there are different adenylate kinases in the compartments | + | <StructureSection load='1ak2' size='340' side='right'caption='[[1ak2]], [[Resolution|resolution]] 1.92Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1ak2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AK2 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]] 1.92Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1ak2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ak2 OCA], [https://pdbe.org/1ak2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ak2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ak2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ak2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/KAD2_BOVIN KAD2_BOVIN] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth. Plays a key role in hematopoiesis (By similarity). | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ak/1ak2_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1ak2 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In vertebrates, there are different adenylate kinases in the compartments cytosol, mitochondrial intermembrane space, and mitochondrial matrix. Here, we report the spatial structure of the intermembrane species established in two crystal forms by X-ray diffraction analyses at 1.92 and 2.1 A resolution. In both structures, the enzyme is unligated, and thus in an "open" conformation. The enzyme was prepared from bovine liver, containing at least five variants arisen from posttranscriptional and posttranslational modifications. It could only be crystallized after removing some of these variants. A comparison with the known structures of the adenylate kinases from cytosol and mitochondrial matrix reveals structural differences that should play a role in protein targeting because none of these enzymes contains a cleavable signal peptide. A further comparison with adenylate kinases from Gram-positive bacteria showed that the structural Zn2+ ion of these species is replaced by a strictly conserved assembly of hydrogen bonded residues. | ||
| - | + | The structure of bovine mitochondrial adenylate kinase: comparison with isoenzymes in other compartments.,Schlauderer GJ, Schulz GE Protein Sci. 1996 Mar;5(3):434-41. PMID:8868479<ref>PMID:8868479</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1ak2" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bos taurus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Schlauderer GJ]] | ||
| + | [[Category: Schulz GE]] | ||
Current revision
ADENYLATE KINASE ISOENZYME-2
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