1ak2
From Proteopedia
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| - | [[Image:1ak2.gif|left|200px]] | + | [[Image:1ak2.gif|left|200px]] |
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| - | '''ADENYLATE KINASE ISOENZYME-2''' | + | {{Structure |
| + | |PDB= 1ak2 |SIZE=350|CAPTION= <scene name='initialview01'>1ak2</scene>, resolution 1.92Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ADENYLATE KINASE ISOENZYME-2''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AK2 is a [ | + | 1AK2 is a [[Single protein]] structure of sequence from [http://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]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8868479 8868479] |
[[Category: Adenylate kinase]] | [[Category: Adenylate kinase]] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
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[[Category: phosphotransferase]] | [[Category: phosphotransferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:58:41 2008'' |
Revision as of 07:58, 20 March 2008
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| , resolution 1.92Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Adenylate kinase, with EC number 2.7.4.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ADENYLATE KINASE ISOENZYME-2
Overview
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.
About this Structure
1AK2 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 09:58:41 2008
