1nb2

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(New page: 200px<br /><applet load="1nb2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nb2, resolution 2.2&Aring;" /> '''Crystal Structure of ...)
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'''Crystal Structure of Nucleoside Diphosphate Kinase from Bacillus Halodenitrificans'''<br />
'''Crystal Structure of Nucleoside Diphosphate Kinase from Bacillus Halodenitrificans'''<br />
==Overview==
==Overview==
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We found that when grown under anaerobic conditions the moderate, halophile, gram-positive bacterium Bacillus halodenitrificans (ATCC 49067), synthesizes large amounts of a polypeptide complex that contains a heme, center capable of reversibly bind nitric oxide. This complex, when exposed, to air, dissociates and reassociates into two active components, a, Mn-containing superoxide dismutase (SOD) and a nucleoside diphosphate, kinase (BhNDK). The crystal structure of this latter enzyme has been, determined at 2.2A resolution using molecular replacement method, based on, the crystal structure of Drosophila melanogaster NDK. The model contains, 149 residues of a total 150 residues and 34 water molecules. BhNDK, consists of a four-stranded antiparallel beta-sheet, whose surfaces are, partially covered by six alpha-helices, and its overall and active site, structures are similar to those of homologous enzymes. However, the, hexameric packing of BhNDK shows that this enzyme is different from both, eukaryotic and gram-negative bacteria. The need for the bacterium to, presynthesize both SOD and NDK precursors which are activated during the, anaerobic-aerobic transition is discussed.
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We found that when grown under anaerobic conditions the moderate halophile, gram-positive bacterium Bacillus halodenitrificans (ATCC 49067) synthesizes large amounts of a polypeptide complex that contains a heme center capable of reversibly bind nitric oxide. This complex, when exposed to air, dissociates and reassociates into two active components, a Mn-containing superoxide dismutase (SOD) and a nucleoside diphosphate kinase (BhNDK). The crystal structure of this latter enzyme has been determined at 2.2A resolution using molecular replacement method, based on the crystal structure of Drosophila melanogaster NDK. The model contains 149 residues of a total 150 residues and 34 water molecules. BhNDK consists of a four-stranded antiparallel beta-sheet, whose surfaces are partially covered by six alpha-helices, and its overall and active site structures are similar to those of homologous enzymes. However, the hexameric packing of BhNDK shows that this enzyme is different from both eukaryotic and gram-negative bacteria. The need for the bacterium to presynthesize both SOD and NDK precursors which are activated during the anaerobic-aerobic transition is discussed.
==About this Structure==
==About this Structure==
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1NB2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Virgibacillus_halodenitrificans Virgibacillus halodenitrificans]. Active as [http://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NB2 OCA].
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1NB2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Virgibacillus_halodenitrificans Virgibacillus halodenitrificans]. Active as [http://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NB2 OCA].
==Reference==
==Reference==
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[[Category: Virgibacillus halodenitrificans]]
[[Category: Virgibacillus halodenitrificans]]
[[Category: Chang, T.]]
[[Category: Chang, T.]]
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[[Category: Chang, W.C.]]
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[[Category: Chang, W C.]]
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[[Category: Chen, C.J.]]
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[[Category: Chen, C J.]]
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[[Category: Gall, J.Le.]]
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[[Category: Gall, J Le.]]
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[[Category: Liu, M.Y.]]
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[[Category: Liu, M Y.]]
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[[Category: Wang, B.C.]]
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[[Category: Wang, B C.]]
[[Category: bacillus halodenitrifians]]
[[Category: bacillus halodenitrifians]]
[[Category: nucleoside diphosphate kinase]]
[[Category: nucleoside diphosphate kinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:09 2008''

Revision as of 12:04, 21 February 2008


1nb2, resolution 2.2Å

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Crystal Structure of Nucleoside Diphosphate Kinase from Bacillus Halodenitrificans

Overview

We found that when grown under anaerobic conditions the moderate halophile, gram-positive bacterium Bacillus halodenitrificans (ATCC 49067) synthesizes large amounts of a polypeptide complex that contains a heme center capable of reversibly bind nitric oxide. This complex, when exposed to air, dissociates and reassociates into two active components, a Mn-containing superoxide dismutase (SOD) and a nucleoside diphosphate kinase (BhNDK). The crystal structure of this latter enzyme has been determined at 2.2A resolution using molecular replacement method, based on the crystal structure of Drosophila melanogaster NDK. The model contains 149 residues of a total 150 residues and 34 water molecules. BhNDK consists of a four-stranded antiparallel beta-sheet, whose surfaces are partially covered by six alpha-helices, and its overall and active site structures are similar to those of homologous enzymes. However, the hexameric packing of BhNDK shows that this enzyme is different from both eukaryotic and gram-negative bacteria. The need for the bacterium to presynthesize both SOD and NDK precursors which are activated during the anaerobic-aerobic transition is discussed.

About this Structure

1NB2 is a Single protein structure of sequence from Virgibacillus halodenitrificans. Active as Nucleoside-diphosphate kinase, with EC number 2.7.4.6 Full crystallographic information is available from OCA.

Reference

Crystal structure of a nucleoside diphosphate kinase from Bacillus halodenitrificans: coexpression of its activity with a Mn-superoxide dismutase., Chen CJ, Liu MY, Chang T, Chang WC, Wang BC, Le Gall J, J Struct Biol. 2003 May;142(2):247-55. PMID:12713952

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