1p99
From Proteopedia
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'''1.7A crystal structure of protein PG110 from Staphylococcus aureus''' | '''1.7A crystal structure of protein PG110 from Staphylococcus aureus''' | ||
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[[Category: Zhang, R.]] | [[Category: Zhang, R.]] | ||
[[Category: Zhou, M.]] | [[Category: Zhou, M.]] | ||
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| - | [[Category: | + | [[Category: Midwest center for structural genomic]] |
| - | [[Category: | + | [[Category: Protein structure initiative]] |
| - | [[Category: | + | [[Category: Psi]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:50:34 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 01:50, 3 May 2008
1.7A crystal structure of protein PG110 from Staphylococcus aureus
Overview
Bacterial dipeptide ABC transporters function to import a wide range of dipeptide substrates. This ability to transport a wide variety of dipeptides is conferred by the cognate substrate binding protein (SBP) of these transporters. SBPs bind dipeptides with little regard for their amino acid content. Here, we report the 1.7 A resolution structure of lipoprotein-9 (SA0422) of Staphylococcus aureus in complex with the dipeptide glycylmethionine. Experimental characterization of the subcellular location of the protein confirmed that SA0422 is an acylated, peripheral membrane protein. This is the first structure determined for an SBP of a Gram-positive dipeptide ABC transporter. Usually, binding of dipeptides occurs in a binding pocket that is largely hydrated and able to accommodate the side chains of several different amino acid residues. Unlike any other known SBP, lipoprotein-9 binds the side chains of the glycylmethionine dipeptide through very specific interactions. Lipoprotein-9 shares significant structural and sequence homology with the MetQ family of methionine SBP. Sequence comparisons between MetQ-like proteins and lipoprotein-9 suggest that the residues forming the tight interactions with the methionine side chains of the ligand are highly conserved between lipoprotein-9 and MetQ homologues, while the residues involved in coordinating the glycine residue are not. Modeling of the Vibrio cholerae MetQ and lipoprotein-9 binding pockets can account for lipoprotein-9 substrate specificity toward glycylmethionine. For this reason, we have designated lipoprotein-9 GmpC, for glycylmethionine binding protein.
About this Structure
1P99 is a Single protein structure of sequence from Staphylococcus aureus subsp. aureus mu50. Full crystallographic information is available from OCA.
Reference
The membrane-associated lipoprotein-9 GmpC from Staphylococcus aureus binds the dipeptide GlyMet via side chain interactions., Williams WA, Zhang RG, Zhou M, Joachimiak G, Gornicki P, Missiakas D, Joachimiak A, Biochemistry. 2004 Dec 28;43(51):16193-202. PMID:15610013 Page seeded by OCA on Sat May 3 04:50:34 2008
