3pte: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:3pte.gif|left|200px]]
[[Image:3pte.png|left|200px]]


<!--
<!--
Line 12: Line 12:




==Overview==
{{ABSTRACT_7490745}}
The D-alanyl-D-alanine peptidase from Streptomyces sp. R61 is a 37,500 dalton exocellular enzyme that has served as a model for membrane-bound peptidases that are involved in bacterial cell wall biosynthesis. Inhibition of these enzymes by beta-lactam antibiotics ultimately leads to bacterial cell death. The X-ray crystal structure of the R61 D-alanyl-D-alanine peptidase has been solved using multiple isomorphous replacement, simulated annealing and least squares refinement. The space group and unit cell parameters are P2(1)2(1)2(1) with a = 51.1 A, b = 67.3 A and c = 102.4 A. The structure has been refined using 2 sigma data to 1.6 A resolution with a crystallographic R-factor of 0.148. The model contains 347 residues (2938 atoms) and 254 solvent molecules. The overall temperature factor is 9.6 A2, and the estimated coordinate error is 0.14 A. The protein consists of a single polypeptide chain organized into two regions. One region contains a nine-stranded antiparallel beta-sheet with helices on both faces; this region includes both the amino and carboxyl termini. The second region is all helical. Sixty percent of the residues occur in helices or beta-sheet. The reactive Ser62 is found between the two regions of the enzyme at the amino end of the protein's longest-helix which begins with one turn of 3(10) helix and continues with four turns of alpha-helix. The active site is an elongated pocket that contains four basic and four aromatic residues. An oxyanion hole is formed by Ser62 NH and Thr301 NH. The pocket also contains the few key residues that are conserved in all penicillin-binding proteins and beta-lactamases. Two of these residues, Lys65 and Tyr159, are among the 16 side-chains that take on multiple conformations in the R61 crystal structure. Three of the 12 proline rings adopt two conformations which we believe has not been previously reported. There is no anionic acid equivalent to the catalytic Glu166 found in Class A beta-lactamases. Two ordered water molecules (O507 and O644) are found buried in the active site and hydrogen-bonded to each other (2.6 A). O507 could potentially act as the hydrolytic water molecule for deacylation.


==About this Structure==
==About this Structure==
3PTE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1pte 1pte]. The following page contains interesting information on the relation of 3PTE with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb29_1.html Penicillin-binding Proteins]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PTE OCA].  
3PTE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1pte 1pte]. The following page contains interesting information on the relation of 3PTE with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb29_1.html Penicillin-binding Proteins]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PTE OCA].  
==Reference==
The refined crystallographic structure of a DD-peptidase penicillin-target enzyme at 1.6 A resolution., Kelly JA, Kuzin AP, J Mol Biol. 1995 Nov 24;254(2):223-36. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7490745 7490745]
[[Category: Penicillin-binding Proteins]]
[[Category: Penicillin-binding Proteins]]
[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
Line 28: Line 24:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Transpeptidase]]
[[Category: Transpeptidase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:11:24 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 18:28:06 2008''

Revision as of 15:28, 26 June 2008

File:3pte.png

Template:STRUCTURE 3pte

THE REFINED CRYSTALLOGRAPHIC STRUCTURE OF A DD-PEPTIDASE PENICILLIN-TARGET ENZYME AT 1.6 A RESOLUTION


Template:ABSTRACT 7490745

About this Structure

3PTE is a Single protein structure of sequence from Streptomyces sp.. This structure supersedes the now removed PDB entry 1pte. The following page contains interesting information on the relation of 3PTE with [Penicillin-binding Proteins]. Full crystallographic information is available from OCA.

Page seeded by OCA on Thu Jun 26 18:28:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=3pte&oldid=568834"