1p31
From Proteopedia
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| - | [[Image:1p31.jpg|left|200px]] | + | [[Image:1p31.jpg|left|200px]] |
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| - | '''Crystal Structure of UDP-N-acetylmuramic acid:L-alanine Ligase (MurC) from Haemophilus influenzae''' | + | {{Structure |
| + | |PDB= 1p31 |SIZE=350|CAPTION= <scene name='initialview01'>1p31</scene>, resolution 1.85Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=EPU:URIDINE-DIPHOSPHATE-2(N-ACETYLGLUCOSAMINYL) BUTYRIC ACID'>EPU</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/UDP-N-acetylmuramate--L-alanine_ligase UDP-N-acetylmuramate--L-alanine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.8 6.3.2.8] | ||
| + | |GENE= MURC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of UDP-N-acetylmuramic acid:L-alanine Ligase (MurC) from Haemophilus influenzae''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1P31 is a [ | + | 1P31 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P31 OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structures of active fully assembled substrate- and product-bound complexes of UDP-N-acetylmuramic acid:L-alanine ligase (MurC) from Haemophilus influenzae., Mol CD, Brooun A, Dougan DR, Hilgers MT, Tari LW, Wijnands RA, Knuth MW, McRee DE, Swanson RV, J Bacteriol. 2003 Jul;185(14):4152-62. PMID:[http:// | + | Crystal structures of active fully assembled substrate- and product-bound complexes of UDP-N-acetylmuramic acid:L-alanine ligase (MurC) from Haemophilus influenzae., Mol CD, Brooun A, Dougan DR, Hilgers MT, Tari LW, Wijnands RA, Knuth MW, McRee DE, Swanson RV, J Bacteriol. 2003 Jul;185(14):4152-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12837790 12837790] |
[[Category: Haemophilus influenzae]] | [[Category: Haemophilus influenzae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: alpha/beta protein]] | [[Category: alpha/beta protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:19:12 2008'' |
Revision as of 11:19, 20 March 2008
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| , resolution 1.85Å | |||||||
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| Ligands: | and | ||||||
| Gene: | MURC (Haemophilus influenzae) | ||||||
| Activity: | UDP-N-acetylmuramate--L-alanine ligase, with EC number 6.3.2.8 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of UDP-N-acetylmuramic acid:L-alanine Ligase (MurC) from Haemophilus influenzae
Overview
UDP-N-acetylmuramic acid:L-alanine ligase (MurC) catalyzes the addition of the first amino acid to the cytoplasmic precursor of the bacterial cell wall peptidoglycan. The crystal structures of Haemophilus influenzae MurC in complex with its substrate UDP-N-acetylmuramic acid (UNAM) and Mg(2+) and of a fully assembled MurC complex with its product UDP-N-acetylmuramoyl-L-alanine (UMA), the nonhydrolyzable ATP analogue AMPPNP, and Mn(2+) have been determined to 1.85- and 1.7-A resolution, respectively. These structures reveal a conserved, three-domain architecture with the binding sites for UNAM and ATP formed at the domain interfaces: the N-terminal domain binds the UDP portion of UNAM, and the central and C-terminal domains form the ATP-binding site, while the C-terminal domain also positions the alanine. An active enzyme structure is thus assembled at the common domain interfaces when all three substrates are bound. The MurC active site clearly shows that the gamma-phosphate of AMPPNP is positioned between two bound metal ions, one of which also binds the reactive UNAM carboxylate, and that the alanine is oriented by interactions with the positively charged side chains of two MurC arginine residues and the negatively charged alanine carboxyl group. These results indicate that significant diversity exists in binding of the UDP moiety of the substrate by MurC and the subsequent ligases in the bacterial cell wall biosynthesis pathway and that alterations in the domain packing and tertiary structure allow the Mur ligases to bind sequentially larger UNAM peptide substrates.
About this Structure
1P31 is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
Crystal structures of active fully assembled substrate- and product-bound complexes of UDP-N-acetylmuramic acid:L-alanine ligase (MurC) from Haemophilus influenzae., Mol CD, Brooun A, Dougan DR, Hilgers MT, Tari LW, Wijnands RA, Knuth MW, McRee DE, Swanson RV, J Bacteriol. 2003 Jul;185(14):4152-62. PMID:12837790
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