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Membrane protein, transferase PDB-id
2fff
Biological unit* = asymmetric unit, as shown
(*as deduced by PQS)
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Protein chains
15 a.a.
453 a.a. *
Metal ions
_NI
Waters ×232

* Residue conservation analysis
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PDB id: 2fff
Name: Membrane protein, transferase
Title: Open form of a class a transpeptidase domain

Structure:
Penicillin-binding protein 1b. Chain: a. Fragment: residues 105-119. Engineered: yes. Penicillin-binding protein 1b. Chain: b. Fragment: transpeptidase domain, residues 337-789. Engineered: yes

Source:
Streptococcus pneumoniae. Organism_taxid: 1313. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Biological unit:
Dimer (from PQS)

UniProt:
Chain A: Q4TUQ1 (Q4TUQ1_STRPN)
Pfam  
Seq:
Struc:
Seq:
Struc:
Seq: 751 a.a.
Struc: 15 a.a.

Chain B: O70038 (O70038_STRPN)
Pfam  
Seq:
Struc:
Seq:
Struc:
Seq:
Struc:
Seq: 821 a.a.
Struc: 453 a.a.
Key:    PfamA domain  PfamB domain
 Secondary structure

Resolution:
2.23Å

R-factor:
0.186

R-free:
0.246

Authors:
A.L.Lovering,N.C.J.Strynadka

Key ref:
A.L.Lovering et al. (2006). Structural analysis of an "open" form of PBP1B from Streptococcus pneumoniae.. Protein Sci, 15, 1701-1709. [PubMed id: 16751607] [DOI: 10.1110/ps.062112106]

Date:
19-Dec-05

Release date:
20-Jun-06
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    Key reference    
 
 
DOI no: 10.1110/ps.062112106 Protein Sci 15:1701-1709 (2006)
PubMed id: 16751607  
 
 
Structural analysis of an "open" form of PBP1B from Streptococcus pneumoniae.
A.L.Lovering, L.De Castro, D.Lim, N.C.Strynadka.
 
  ABSTRACT  
 
The class A PBP1b from Streptococcus pneumoniae is responsible for glycosyltransferase and transpeptidase (TP) reactions, forming the peptidoglycan of the bacterial cell wall. The enzyme has been produced in a stable, soluble form and undergoes time-dependent proteolysis to leave an intact TP domain. Crystals of this TP domain were obtained, diffracting to 2.2 A resolution, and the structure was solved by using molecular replacement. Analysis of the structure revealed an "open" active site, with important conformational differences to the previously determined "closed" apoenzyme. The active-site nucleophile, Ser460, is in an orientation that allows for acylation by beta-lactams. Consistent with the productive conformation of the conserved active-site catalytic residues, adjacent loops show only minor deviation from those of known acyl-enzyme structures. These findings are discussed in the context of enzyme functionality and the possible conformational sampling of PBP1b between active and inactive states.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18266856 E.Sauvage, F.Kerff, M.Terrak, J.A.Ayala, and P.Charlier (2008).
The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis.
  FEMS Microbiol Rev, 32, 234-258.  
18337244 S.Lemaire, C.Fuda, F.Van Bambeke, P.M.Tulkens, and S.Mobashery (2008).
Restoration of susceptibility of methicillin-resistant Staphylococcus aureus to beta-lactam antibiotics by acidic pH: role of penicillin-binding protein PBP 2a.
  J Biol Chem, 283, 12769-12776.  
17724158 M.Yamada, T.Watanabe, T.Miyara, N.Baba, J.Saito, Y.Takeuchi, and F.Ohsawa (2007).
Crystal structure of cefditoren complexed with Streptococcus pneumoniae penicillin-binding protein 2X: structural basis for its high antimicrobial activity.
  Antimicrob Agents Chemother, 51, 3902-3907.
PDB codes: 2z2l 2z2m
17360321 Y.Yuan, D.Barrett, Y.Zhang, D.Kahne, P.Sliz, and S.Walker (2007).
Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis.
  Proc Natl Acad Sci U S A, 104, 5348-5353.
PDB code: 2oqo
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.