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1uxy

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[[Image:1uxy.jpg|left|200px]]<br /><applet load="1uxy" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1uxy.jpg|left|200px]]
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caption="1uxy, resolution 1.80&Aring;" />
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'''MURB MUTANT WITH SER 229 REPLACED BY ALA, COMPLEX WITH ENOLPYRUVYL-UDP-N-ACETYLGLUCOSAMINE'''<br />
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{{Structure
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|PDB= 1uxy |SIZE=350|CAPTION= <scene name='initialview01'>1uxy</scene>, resolution 1.80&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=EPU:URIDINE-DIPHOSPHATE-2(N-ACETYLGLUCOSAMINYL) BUTYRIC ACID'>EPU</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''MURB MUTANT WITH SER 229 REPLACED BY ALA, COMPLEX WITH ENOLPYRUVYL-UDP-N-ACETYLGLUCOSAMINE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1UXY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=EPU:'>EPU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1UXY OCA].
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1UXY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UXY OCA].
==Reference==
==Reference==
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X-ray crystal structures of the S229A mutant and wild-type MurB in the presence of the substrate enolpyruvyl-UDP-N-acetylglucosamine at 1.8-A resolution., Benson TE, Walsh CT, Hogle JM, Biochemistry. 1997 Jan 28;36(4):806-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9020778 9020778]
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X-ray crystal structures of the S229A mutant and wild-type MurB in the presence of the substrate enolpyruvyl-UDP-N-acetylglucosamine at 1.8-A resolution., Benson TE, Walsh CT, Hogle JM, Biochemistry. 1997 Jan 28;36(4):806-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9020778 9020778]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: peptidoglycan synthesis]]
[[Category: peptidoglycan synthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:29:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:38:20 2008''

Revision as of 12:38, 20 March 2008


PDB ID 1uxy

Drag the structure with the mouse to rotate
, resolution 1.80Å
Ligands: and
Activity: UDP-N-acetylmuramate dehydrogenase, with EC number 1.1.1.158
Coordinates: save as pdb, mmCIF, xml



MURB MUTANT WITH SER 229 REPLACED BY ALA, COMPLEX WITH ENOLPYRUVYL-UDP-N-ACETYLGLUCOSAMINE


Overview

MurB catalyzes the second committed step in the synthesis of peptidoglycan, a key component of the bacterial cell wall. The crystal structures of both a S229A mutant and wild-type MurB in the presence of the substrate enolpyruvyl-UDP-N-acetylglucosamine were solved and refined at 1.8 A resolution. The single point mutation of residue 229 from serine to alanine eliminated a hydroxyl group which has previously been proposed to play a critical role as a proton donor during the second half-reaction of MurB, namely, reoxidation of FADH2 and reduction of the enolpyruvyl substrate. The mutation also resulted in the loss of the water molecule-hydrogen bonded to the serine hydroxyl in the wild-type structure changing the hydrogen-bonding network with in the active site. Comparison of the wild-type and S229A mutant structures confirms that the dramatic kinetic defect of an approximately 10(7)-fold decrease observed for the Ser 229 Ala mutant in the second half-reaction [Benson, T.E., Walsh, C.T., & Massey, V. (1997) Biochemistry 36, 796-805] is a direct result of the loss of the serine hydroxyl moiety rather than other nonspecific active-site changes or general structural defects.

About this Structure

1UXY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

X-ray crystal structures of the S229A mutant and wild-type MurB in the presence of the substrate enolpyruvyl-UDP-N-acetylglucosamine at 1.8-A resolution., Benson TE, Walsh CT, Hogle JM, Biochemistry. 1997 Jan 28;36(4):806-11. PMID:9020778

Page seeded by OCA on Thu Mar 20 14:38:20 2008

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