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PDBsum entry 1jjw
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protein metals Protein-protein interface(s) links
Hydrolase PDB id
1jjw

 

 

 

 

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Contents
Protein chains
173 a.a. *
Metals
__K ×3
Waters ×191
* Residue conservation analysis
PDB id:
1jjw
Name: Hydrolase
Title: Structure of haemophilus influenzae hslv protein at 1.9 a resolution
Structure: Atp-dependent protease hslv. Chain: a, b, c. Engineered: yes
Source: Haemophilus influenzae. Organism_taxid: 727. Gene: hslv. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Biol. unit: Dodecamer (from PDB file)
Resolution:
1.90Å     R-factor:   0.215     R-free:   0.249
Authors: M.C.Sousa,D.B.Mckay
Key ref:
M.C.Sousa and D.B.McKay (2001). Structure of Haemophilus influenzae HslV protein at 1.9 A resolution, revealing a cation-binding site near the catalytic site. Acta Crystallogr D Biol Crystallogr, 57, 1950-1954. PubMed id: 11717526 DOI: 10.1107/S090744490101575X
Date:
09-Jul-01     Release date:   05-Dec-01    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P43772  (HSLV_HAEIN) -  ATP-dependent protease subunit HslV from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Seq:
Struc: 		175 a.a.
173 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.25.2  - HslU--HslV peptidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1107/S090744490101575X Acta Crystallogr D Biol Crystallogr 57:1950-1954 (2001)
PubMed id: 11717526  
 
 
Structure of Haemophilus influenzae HslV protein at 1.9 A resolution, revealing a cation-binding site near the catalytic site.
M.C.Sousa, D.B.McKay.
 
  ABSTRACT  
 
The structure of the Haemophilus influenzae HslV protease of the HslUV 'prokaryotic proteasome' has been solved by molecular replacement and refined with data to 1.9 A resolution. The protease is a 'double donut' of hexameric rings; two alternative sets of intermolecular interactions between protomers in the rings result in 'quasi-equivalent' packing within the assembly. Anomalous scattering data from crystals with potassium present in the mother liquor reveal a K(+) ion bound with octahedral coordination near the active-site Thr1 residue. The site also binds Na(+) ions and is likely to bind Mg(2+), suggesting that monovalent and divalent metal ions may influence the catalytic activity of the protease.
 
  Selected figure(s)  
 
Figure 1.
Figure 1 Quasi-equivalent subunit interactions within HslV. (a) Ribbon drawing of one hexamer, looking down the pseudo-sixfold axis. Subunits related by crystallographic twofold rotation are shown in identical colors and denoted with a prime. Regions on the apical helices which reveal differences in subunit-subunit interactions are highlighted: magenta on cyan for subunit A; red on yellow for subunit B; green on gold for subunit C. (b) Interactions between subunits C and A, using same color coding as in (a). (c) Interactions between subunits B and C. Figs. 1-and 2-(b) were produced with MOLSCRIPT (Kraulis, 1991[Kraulis, P. (1991). J. Appl. Cryst. 24, 946-950.]) and Fig. 2-(a) was produced with BOBSCRIPT (Esnouf, 1997[Esnouf, R. M. (1997). J. Mol. Graph. 15, 132-134.], 1999[Esnouf, R. M. (1999). Acta Cryst. D55, 938-940.]); all figures were rendered with Raster3D (Merritt & Bacon, 1997[Merritt, E. A. & Bacon, D. J. (1997). Methods Enzymol. 277, 505-524.]).
 
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2001, 57, 1950-1954) copyright 2001.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18582897 J.A.Yakamavich, T.A.Baker, and R.T.Sauer (2008).
Asymmetric nucleotide transactions of the HslUV protease.
  J Mol Biol, 380, 946-957.  
16901897 S.Adhikari, J.A.Toretsky, L.Yuan, and R.Roy (2006).
Magnesium, essential for base excision repair enzymes, inhibits substrate binding of N-methylpurine-DNA glycosylase.
  J Biol Chem, 281, 29525-29532.  
15678420 M.Groll, M.Bochtler, H.Brandstetter, T.Clausen, and R.Huber (2005).
Molecular machines for protein degradation.
  Chembiochem, 6, 222-256.  
15064753 S.A.Joshi, G.L.Hersch, T.A.Baker, and R.T.Sauer (2004).
Communication between ClpX and ClpP during substrate processing and degradation.
  Nat Struct Mol Biol, 11, 404-411.  
14675543 M.Groll, and T.Clausen (2003).
Molecular shredders: how proteasomes fulfill their role.
  Curr Opin Struct Biol, 13, 665-673.  
14612565 S.Prasad, K.J.Wright, D.Banerjee Roy, L.A.Bush, A.M.Cantwell, and E.Di Cera (2003).
Redesigning the monovalent cation specificity of an enzyme.
  Proc Natl Acad Sci U S A, 100, 13785-13790.  
12032294 R.Ramachandran, C.Hartmann, H.K.Song, R.Huber, and M.Bochtler (2002).
Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY).
  Proc Natl Acad Sci U S A, 99, 7396-7401.  
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.

 

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