1zak: Difference between revisions

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[[Image:1zak.jpg|left|200px]]
[[Image:1zak.jpg|left|200px]]


{{Structure
<!--
|PDB= 1zak |SIZE=350|CAPTION= <scene name='initialview01'>1zak</scene>, resolution 3.5&Aring;
The line below this paragraph, containing "STRUCTURE_1zak", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=AP5:BIS(ADENOSINE)-5&#39;-PENTAPHOSPHATE'>AP5</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <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>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_1zak| PDB=1zak  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zak OCA], [http://www.ebi.ac.uk/pdbsum/1zak PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zak RCSB]</span>
}}


'''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)'''
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[[Category: Schulz, G E.]]
[[Category: Schulz, G E.]]
[[Category: Wild, K.]]
[[Category: Wild, K.]]
[[Category: atp:amp-phosphotransferase]]
[[Category: Atp:amp-phosphotransferase]]
[[Category: transferase]]
[[Category: Transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:23:33 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:33:12 2008''

Revision as of 17:23, 3 May 2008

File:1zak.jpg

Template:STRUCTURE 1zak

ADENYLATE KINASE FROM MAIZE IN COMPLEX WITH THE INHIBITOR P1,P5-BIS(ADENOSINE-5'-)PENTAPHOSPHATE (AP5A)


OverviewOverview

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.

About this StructureAbout this Structure

1ZAK is a Single protein structure of sequence from Zea mays. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Sat May 3 17:23:33 2008

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