1p4n

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(New page: 200px<br /><applet load="1p4n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p4n, resolution 1.90&Aring;" /> '''Crystal Structure of...)
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'''Crystal Structure of Weissella viridescens FemX:UDP-MurNAc-pentapeptide complex'''<br />
'''Crystal Structure of Weissella viridescens FemX:UDP-MurNAc-pentapeptide complex'''<br />
==Overview==
==Overview==
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Members of the FemABX protein family are novel therapeutic targets, as, they are involved in the synthesis of the bacterial cell wall. They, catalyze the addition of amino acid(s) on the peptidoglycan precursor, using aminoacylated tRNA as a substrate. We report here the, high-resolution structure of Weissella viridescens L-alanine transferase, FemX and its complex with the UDP-MurNAc-pentapeptide. This is the first, structure example of a FemABX family member that does not possess a, coiled-coil domain. FemX consists of two structurally equivalent domains, separated by a cleft containing the binding site of the, UDP-MurNAc-pentapeptide and a long channel that traverses one of the two, domains. Our structural studies bring new insights into the evolution of, the FemABX and the related GNAT superfamilies, shed light on the, recognition site of the aminoacylated tRNA in Fem proteins, and allowed, manual docking of the acceptor end of the alanyl-tRNAAla.
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Members of the FemABX protein family are novel therapeutic targets, as they are involved in the synthesis of the bacterial cell wall. They catalyze the addition of amino acid(s) on the peptidoglycan precursor using aminoacylated tRNA as a substrate. We report here the high-resolution structure of Weissella viridescens L-alanine transferase FemX and its complex with the UDP-MurNAc-pentapeptide. This is the first structure example of a FemABX family member that does not possess a coiled-coil domain. FemX consists of two structurally equivalent domains, separated by a cleft containing the binding site of the UDP-MurNAc-pentapeptide and a long channel that traverses one of the two domains. Our structural studies bring new insights into the evolution of the FemABX and the related GNAT superfamilies, shed light on the recognition site of the aminoacylated tRNA in Fem proteins, and allowed manual docking of the acceptor end of the alanyl-tRNAAla.
==About this Structure==
==About this Structure==
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1P4N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Weissella_viridescens Weissella viridescens] with MG and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylmuramoylpentapeptide-lysine_N(6)-alanyltransferase UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.10 2.3.2.10] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P4N OCA].
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1P4N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Weissella_viridescens Weissella viridescens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylmuramoylpentapeptide-lysine_N(6)-alanyltransferase UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.10 2.3.2.10] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P4N OCA].
==Reference==
==Reference==
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[[Category: ligase]]
[[Category: ligase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:58:22 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:01 2008''

Revision as of 12:25, 21 February 2008


1p4n, resolution 1.90Å

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Crystal Structure of Weissella viridescens FemX:UDP-MurNAc-pentapeptide complex

Overview

Members of the FemABX protein family are novel therapeutic targets, as they are involved in the synthesis of the bacterial cell wall. They catalyze the addition of amino acid(s) on the peptidoglycan precursor using aminoacylated tRNA as a substrate. We report here the high-resolution structure of Weissella viridescens L-alanine transferase FemX and its complex with the UDP-MurNAc-pentapeptide. This is the first structure example of a FemABX family member that does not possess a coiled-coil domain. FemX consists of two structurally equivalent domains, separated by a cleft containing the binding site of the UDP-MurNAc-pentapeptide and a long channel that traverses one of the two domains. Our structural studies bring new insights into the evolution of the FemABX and the related GNAT superfamilies, shed light on the recognition site of the aminoacylated tRNA in Fem proteins, and allowed manual docking of the acceptor end of the alanyl-tRNAAla.

About this Structure

1P4N is a Single protein structure of sequence from Weissella viridescens with and as ligands. Active as UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase, with EC number 2.3.2.10 Full crystallographic information is available from OCA.

Reference

Crystal structures of Weissella viridescens FemX and its complex with UDP-MurNAc-pentapeptide: insights into FemABX family substrates recognition., Biarrotte-Sorin S, Maillard AP, Delettre J, Sougakoff W, Arthur M, Mayer C, Structure. 2004 Feb;12(2):257-67. PMID:14962386

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