1hsk

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(New page: 200px<br /><applet load="1hsk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hsk, resolution 2.30&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1hsk.gif|left|200px]]<br /><applet load="1hsk" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1hsk.gif|left|200px]]<br /><applet load="1hsk" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1hsk, resolution 2.30&Aring;" />
caption="1hsk, resolution 2.30&Aring;" />
'''CRYSTAL STRUCTURE OF S. AUREUS MURB'''<br />
'''CRYSTAL STRUCTURE OF S. AUREUS MURB'''<br />
==Overview==
==Overview==
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The X-ray crystal structure of the substrate free form of Staphylococcus, aureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB) has been solved, to 2.3 A resolution with an R-factor of 20.3% and a free R-factor of, 22.3%. While the overall fold of the S. aureus enzyme is similar to that, of the homologous Escherichia coli MurB X-ray crystal structure, notable, distinctions between the S. aureus and E. coli MurB protein structures, occur in residues involved in substrate binding. Analysis of available, MurB sequences from other bacteria suggest that the S. aureus MurB, structure is representative of a distinct structural class of, UDP-N-acetylenolpyruvylglucosamine reductases including Bacillus subtilis, and Helicobacter pylori that are characterized by a modified mechanism for, substrate binding.
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The X-ray crystal structure of the substrate free form of Staphylococcus aureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB) has been solved to 2.3 A resolution with an R-factor of 20.3% and a free R-factor of 22.3%. While the overall fold of the S. aureus enzyme is similar to that of the homologous Escherichia coli MurB X-ray crystal structure, notable distinctions between the S. aureus and E. coli MurB protein structures occur in residues involved in substrate binding. Analysis of available MurB sequences from other bacteria suggest that the S. aureus MurB structure is representative of a distinct structural class of UDP-N-acetylenolpyruvylglucosamine reductases including Bacillus subtilis and Helicobacter pylori that are characterized by a modified mechanism for substrate binding.
==About this Structure==
==About this Structure==
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1HSK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with FAD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylmuramate_dehydrogenase UDP-N-acetylmuramate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.158 1.1.1.158] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HSK OCA].
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1HSK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylmuramate_dehydrogenase UDP-N-acetylmuramate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.158 1.1.1.158] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HSK OCA].
==Reference==
==Reference==
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[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: UDP-N-acetylmuramate dehydrogenase]]
[[Category: UDP-N-acetylmuramate dehydrogenase]]
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[[Category: Baldwin, E.T.]]
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[[Category: Baldwin, E T.]]
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[[Category: Benson, T.E.]]
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[[Category: Benson, T E.]]
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[[Category: Choi, G.H.]]
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[[Category: Choi, G H.]]
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[[Category: Cialdella, J.I.]]
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[[Category: Cialdella, J I.]]
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[[Category: Harris, M.S.]]
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[[Category: Harris, M S.]]
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[[Category: Herberg, J.T.]]
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[[Category: Herberg, J T.]]
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[[Category: Jr., J.P.Martin.]]
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[[Category: Jr., J P.Martin.]]
[[Category: FAD]]
[[Category: FAD]]
[[Category: cell division]]
[[Category: cell division]]
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[[Category: peptidoglycan synthesis]]
[[Category: peptidoglycan synthesis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:47:55 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:24 2008''

Revision as of 11:04, 21 February 2008


1hsk, resolution 2.30Å

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CRYSTAL STRUCTURE OF S. AUREUS MURB

Overview

The X-ray crystal structure of the substrate free form of Staphylococcus aureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB) has been solved to 2.3 A resolution with an R-factor of 20.3% and a free R-factor of 22.3%. While the overall fold of the S. aureus enzyme is similar to that of the homologous Escherichia coli MurB X-ray crystal structure, notable distinctions between the S. aureus and E. coli MurB protein structures occur in residues involved in substrate binding. Analysis of available MurB sequences from other bacteria suggest that the S. aureus MurB structure is representative of a distinct structural class of UDP-N-acetylenolpyruvylglucosamine reductases including Bacillus subtilis and Helicobacter pylori that are characterized by a modified mechanism for substrate binding.

About this Structure

1HSK is a Single protein structure of sequence from Staphylococcus aureus with as ligand. Active as UDP-N-acetylmuramate dehydrogenase, with EC number 1.1.1.158 Full crystallographic information is available from OCA.

Reference

A structural variation for MurB: X-ray crystal structure of Staphylococcus aureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB)., Benson TE, Harris MS, Choi GH, Cialdella JI, Herberg JT, Martin JP Jr, Baldwin ET, Biochemistry. 2001 Feb 27;40(8):2340-50. PMID:11327854

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