1ejd: Difference between revisions
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[[Image:1ejd.gif|left|200px]] | [[Image:1ejd.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF UNLIGANDED MURA (TYPE1)''' | {{Structure | ||
|PDB= 1ejd |SIZE=350|CAPTION= <scene name='initialview01'>1ejd</scene>, resolution 1.55Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=HAI:CYCLOHEXYLAMMONIUM ION'>HAI</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_1-carboxyvinyltransferase UDP-N-acetylglucosamine 1-carboxyvinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.7 2.5.1.7] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF UNLIGANDED MURA (TYPE1)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1EJD is a [ | 1EJD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EJD OCA]. | ||
==Reference== | ==Reference== | ||
Comparative X-ray analysis of the un-liganded fosfomycin-target murA., Eschenburg S, Schonbrunn E, Proteins. 2000 Aug 1;40(2):290-8. PMID:[http:// | Comparative X-ray analysis of the un-liganded fosfomycin-target murA., Eschenburg S, Schonbrunn E, Proteins. 2000 Aug 1;40(2):290-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10842342 10842342] | ||
[[Category: Enterobacter cloacae]] | [[Category: Enterobacter cloacae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: inside-out alpha/beta barrel]] | [[Category: inside-out alpha/beta barrel]] | ||
''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 10:56:26 2008'' |
Revision as of 11:56, 20 March 2008
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, resolution 1.55Å | |||||||
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Ligands: | and | ||||||
Activity: | UDP-N-acetylglucosamine 1-carboxyvinyltransferase, with EC number 2.5.1.7 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CRYSTAL STRUCTURE OF UNLIGANDED MURA (TYPE1)
OverviewOverview
MurA, an essential enzyme for the synthesis of the bacterial cell wall, follows an induced-fit mechanism. Upon substrate binding, the active site forms in the interdomain cleft, involving movements of the two domains of the protein and a reorientation of the loop Pro112-Pro121. We compare two structures of un-liganded MurA from Enterobacter cloacae: a new orthorhombic form, solved to 1.80 A resolution, and a monoclinic form, redetermined to 1.55 A resolution. In the monoclinic form, the loop Pro112-Pro121 stretches into solvent, while in the new form it adopts a winded conformation, thereby reducing solvent accessibility of the critical residue Cys115. In the interdomain cleft a network of 27 common water molecules has been identified, which partially shields negative charges in the cleft and stabilizes the orientation of catalytically crucial residues. This could support substrate binding and ease domain movements. Near the hinge region an isoaspartyl residue has been recognized, which is the product of post-translational modification of the genetically encoded Asn67-Gly68. The homogeneous population with L-isoaspartate in both structures suggests that the modification in Enterobacter cloacae MurA is not a mere aging defect but rather the result of a specific in vivo process.
About this StructureAbout this Structure
1EJD is a Single protein structure of sequence from Enterobacter cloacae. Full crystallographic information is available from OCA.
ReferenceReference
Comparative X-ray analysis of the un-liganded fosfomycin-target murA., Eschenburg S, Schonbrunn E, Proteins. 2000 Aug 1;40(2):290-8. PMID:10842342
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