1lmh

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|PDB= 1lmh |SIZE=350|CAPTION= <scene name='initialview01'>1lmh</scene>, resolution 1.90&Aring;
|PDB= 1lmh |SIZE=350|CAPTION= <scene name='initialview01'>1lmh</scene>, resolution 1.90&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/N-formylmethionylaminoacyl-tRNA_deformylase N-formylmethionylaminoacyl-tRNA deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.27 3.5.1.27]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/N-formylmethionylaminoacyl-tRNA_deformylase N-formylmethionylaminoacyl-tRNA deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.27 3.5.1.27] </span>
|GENE= DEF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
|GENE= DEF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lmh OCA], [http://www.ebi.ac.uk/pdbsum/1lmh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lmh RCSB]</span>
}}
}}
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[[Category: Baldwin, E T.]]
[[Category: Baldwin, E T.]]
[[Category: Harris, M S.]]
[[Category: Harris, M S.]]
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[[Category: ZN]]
 
[[Category: zinc peptidase]]
[[Category: zinc peptidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:32:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:04:38 2008''

Revision as of 19:04, 30 March 2008


PDB ID 1lmh

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands: ,
Gene: DEF (Staphylococcus aureus)
Activity: N-formylmethionylaminoacyl-tRNA deformylase, with EC number 3.5.1.27
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of S. aureus peptide deformylase


Overview

The first crystal structure of Class II peptide deformylase has been determined. The enzyme from Staphylococcus aureus has been overexpressed and purified in Escherichia coli and the structure determined by x-ray crystallography to 1.9 A resolution. The purified iron-enriched form of S. aureus peptide deformylase enzyme retained high activity over many months. In contrast, the iron-enriched form of the E. coli enzyme is very labile. Comparison of the two structures details many differences; however, there is no structural explanation for the dramatic activity differences we observed. The protein structure of the S. aureus enzyme reveals a fold similar, but not identical to, the well characterized E. coli enzyme. The most striking deviation of the S. aureus from the E. coli structure is the unique conformation of the C-terminal amino acids. The distinctive C-terminal helix of the latter is replaced by a strand in S. aureus which wraps around the enzyme, terminating near the active site. Although there are no differences at the amino acid level near the active site metal ion, significant changes are noted in the peptide binding cleft which may play a role in the design of general peptide deformylase inhibitors.

About this Structure

1LMH is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

Crystal structure of type II peptide deformylase from Staphylococcus aureus., Baldwin ET, Harris MS, Yem AW, Wolfe CL, Vosters AF, Curry KA, Murray RW, Bock JH, Marshall VP, Cialdella JI, Merchant MH, Choi G, Deibel MR Jr, J Biol Chem. 2002 Aug 23;277(34):31163-71. Epub 2002 Jun 4. PMID:12048187

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