1zak: Difference between revisions
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=AP5:BIS(ADENOSINE)-5'-PENTAPHOSPHATE'>AP5</scene> | |LIGAND= <scene name='pdbligand=AP5:BIS(ADENOSINE)-5'-PENTAPHOSPHATE'>AP5</scene> | ||
|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] | |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> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|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> | |||
}} | }} | ||
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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 | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:33:12 2008'' | ||
Revision as of 01:33, 31 March 2008
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| , resolution 3.5Å | |||||||
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| Ligands: | |||||||
| Activity: | Adenylate kinase, with EC number 2.7.4.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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