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.

2mlp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2mlp.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2mlp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2mlp| PDB=2mlp | SCENE= }}
{{STRUCTURE_2mlp| PDB=2mlp | SCENE= }}
-
'''MICROCIN LEADER PEPTIDE FROM E. COLI, NMR, 25 STRUCTURES'''
+
===MICROCIN LEADER PEPTIDE FROM E. COLI, NMR, 25 STRUCTURES===
-
==Overview==
+
<!--
-
BACKGROUND: The peptide antibiotic microcin B17 (MccB17) contains oxazole and thiazole heterocycles formed by the post-translational modification of four cysteine and four serine residues. An amino-terminal propeptide targets the 69 amino acid precursor of MccB17 (preproMccB17) to the heterocyclization enzyme MccB17 synthetase. The mode of synthetase recognition has been unclear, because there has been limited structural information available on the MccB17 propeptide to date. RESULTS: The solution structure of the MccB17 propeptide (McbA1-26), determined using nuclear magnetic resonance, reveals that McbA1-26 is an amphipathic alpha helix. Mutational analysis of 13 propeptide residues showed that Phe8 and Leu12 are essential residues for MccB17 synthetase recognition. A domain of the propeptide was putatively identified as the region that interacts with the synthetase. CONCLUSIONS: MccB17 synthetase recognizes key hydrophobic residues within a helical propeptide, allowing the selective heterocyclization of downstream cysteine and serine residues in preproMccB17. The determination of the solution structure of the propeptide should facilitate the investigation of other functions of the propeptide, including a potential role in antibiotic secretion.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9545435}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9545435 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9545435}}
==About this Structure==
==About this Structure==
-
2MLP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MLP OCA].
+
2MLP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MLP OCA].
==Reference==
==Reference==
Line 29: Line 33:
[[Category: Leader peptide]]
[[Category: Leader peptide]]
[[Category: Propeptide]]
[[Category: Propeptide]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:34:00 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:05:05 2008''

Revision as of 11:05, 27 July 2008

Image:2mlp.png

Template:STRUCTURE 2mlp

MICROCIN LEADER PEPTIDE FROM E. COLI, NMR, 25 STRUCTURES

Template:ABSTRACT PUBMED 9545435

About this Structure

2MLP is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

Reference

Role of the microcin B17 propeptide in substrate recognition: solution structure and mutational analysis of McbA1-26., Roy RS, Kim S, Baleja JD, Walsh CT, Chem Biol. 1998 Apr;5(4):217-28. PMID:9545435

Page seeded by OCA on Sun Jul 27 14:05:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2mlp"
Personal tools