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==ADENYLATE KINASE FROM MAIZE IN COMPLEX WITH THE INHIBITOR P1,P5-BIS(ADENOSINE-5'-)PENTAPHOSPHATE (AP5A)== | |||
<StructureSection load='1zak' size='340' side='right'caption='[[1zak]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1zak]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZAK 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]] 3.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AP5:BIS(ADENOSINE)-5-PENTAPHOSPHATE'>AP5</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=1zak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zak OCA], [https://pdbe.org/1zak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zak RCSB], [https://www.ebi.ac.uk/pdbsum/1zak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zak ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KADC_MAIZE KADC_MAIZE] 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. The maize enzyme also works with CMP, albeit with 10% of the activity with AMP.[HAMAP-Rule:MF_00235] | |||
== 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/za/1zak_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1zak ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of adenylate kinase from maize ligated with an inhibitor has been determined by molecular replacement and refined to 3.5-A resolution. The enzyme keeps the ATP/ADP/AMP equilibrium in the cell. In the C4 plant maize, it has the special task to recycle the AMP produced in large amounts in primary CO2 assimilation. The established structure explains the side reaction with CMP. Moreover, it shows infinite rods that can be readily discerned in the crystal packing. In comparison with homologues, two structural differences that are crucial for this supramolecular assembly are evident. We propose that the rods represent a natural inactive storage form that assembles at night when maize stops CO2 assimilation and thus most of the AMP production in its C4 cycle. The enzyme is particularly abundant in mesophyll chloroplasts, where such an assembly would release appreciable amounts of water that can be used in other processes during the night. | |||
Structure, catalysis and supramolecular assembly of adenylate kinase from maize.,Wild K, Grafmuller R, Wagner E, Schulz GE Eur J Biochem. 1997 Dec 1;250(2):326-31. PMID:9428681<ref>PMID:9428681</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1zak" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Adenylate kinase|Adenylate kinase]] | *[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Zea mays]] | [[Category: Zea mays]] | ||
[[Category: Schulz | [[Category: Schulz GE]] | ||
[[Category: Wild | [[Category: Wild K]] | ||
Latest revision as of 09:39, 9 August 2023
ADENYLATE KINASE FROM MAIZE IN COMPLEX WITH THE INHIBITOR P1,P5-BIS(ADENOSINE-5'-)PENTAPHOSPHATE (AP5A)ADENYLATE KINASE FROM MAIZE IN COMPLEX WITH THE INHIBITOR P1,P5-BIS(ADENOSINE-5'-)PENTAPHOSPHATE (AP5A)
Structural highlights
FunctionKADC_MAIZE 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. The maize enzyme also works with CMP, albeit with 10% of the activity with AMP.[HAMAP-Rule:MF_00235] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of adenylate kinase from maize ligated with an inhibitor has been determined by molecular replacement and refined to 3.5-A resolution. The enzyme keeps the ATP/ADP/AMP equilibrium in the cell. In the C4 plant maize, it has the special task to recycle the AMP produced in large amounts in primary CO2 assimilation. The established structure explains the side reaction with CMP. Moreover, it shows infinite rods that can be readily discerned in the crystal packing. In comparison with homologues, two structural differences that are crucial for this supramolecular assembly are evident. We propose that the rods represent a natural inactive storage form that assembles at night when maize stops CO2 assimilation and thus most of the AMP production in its C4 cycle. The enzyme is particularly abundant in mesophyll chloroplasts, where such an assembly would release appreciable amounts of water that can be used in other processes during the night. Structure, catalysis and supramolecular assembly of adenylate kinase from maize.,Wild K, Grafmuller R, Wagner E, Schulz GE Eur J Biochem. 1997 Dec 1;250(2):326-31. PMID:9428681[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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