1ak2

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(New page: 200px<br /><applet load="1ak2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ak2, resolution 1.92&Aring;" /> '''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"
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[[Image:1ak2.gif|left|200px]]<br /><applet load="1ak2" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ak2, resolution 1.92&Aring;" />
caption="1ak2, resolution 1.92&Aring;" />
'''ADENYLATE KINASE ISOENZYME-2'''<br />
'''ADENYLATE KINASE ISOENZYME-2'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1AK2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AK2 OCA].
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1AK2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AK2 OCA].
==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Schlauderer, G.J.]]
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[[Category: Schlauderer, G J.]]
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[[Category: Schulz, G.E.]]
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[[Category: Schulz, G E.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: nucleoside monophosphate kinase]]
[[Category: nucleoside monophosphate kinase]]
[[Category: phosphotransferase]]
[[Category: phosphotransferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:54:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:45:23 2008''

Revision as of 09:45, 21 February 2008


1ak2, resolution 1.92Å

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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 with as ligand. Active as Adenylate kinase, with EC number 2.7.4.3 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

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