We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1p99

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1p99.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1p99.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1p99| PDB=1p99 | SCENE= }}
{{STRUCTURE_1p99| PDB=1p99 | SCENE= }}
-
'''1.7A crystal structure of protein PG110 from Staphylococcus aureus'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15610013}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15610013 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15610013}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Psi]]
[[Category: Psi]]
[[Category: Structural genomic]]
[[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 Mon Jul 28 09:31:46 2008''

Revision as of 06:31, 28 July 2008

Image:1p99.png

Template:STRUCTURE 1p99

1.7A crystal structure of protein PG110 from Staphylococcus aureus

Template:ABSTRACT PUBMED 15610013

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 Mon Jul 28 09:31:46 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p99"
Personal tools