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Transferase PDB id
1k47
Jmol
Contents
Protein chains
(+ 0 more) 322 a.a. *
Waters ×779
* Residue conservation analysis
PDB id:
1k47
Name: Transferase
Title: Crystal structure of the streptococcus pneumoniae phosphomevalonate kinase (pmk)
Structure: Phosphomevalonate kinase. Chain: a, b, c, d, e, f. Engineered: yes
Source: Streptococcus pneumoniae r6. Organism_taxid: 171101. Strain: atcc baa-255 / r6. Gene: mvak2. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Biol. unit: Dimer (from PQS)
Resolution:
2.42Å     R-factor:   0.215     R-free:   0.257
Authors: M.J.Romanowski,J.B.Bonanno,S.K.Burley,New York Sgx Research Center For Structural Genomics (Nysgxrc)
Key ref:
M.J.Romanowski et al. (2002). Crystal structure of the Streptococcus pneumoniae phosphomevalonate kinase, a member of the GHMP kinase superfamily. Proteins, 47, 568-571. PubMed id: 12001237 DOI: 10.1002/prot.10118.abs
Date:
05-Oct-01     Release date:   08-May-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8DR49  (Q8DR49_STRR6) -  Phosphomevalonate kinase
Seq:
Struc:
335 a.a.
322 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     phosphorylation   1 term 
  Biochemical function     nucleotide binding     4 terms  

 

 
DOI no: 10.1002/prot.10118.abs Proteins 47:568-571 (2002)
PubMed id: 12001237  
 
 
Crystal structure of the Streptococcus pneumoniae phosphomevalonate kinase, a member of the GHMP kinase superfamily.
M.J.Romanowski, J.B.Bonanno, S.K.Burley.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. Alignment of S. pneumoniae PMK homologs and related proteins identified during an iterative PSI-BLAST[14] search (20 iterations; January 2002). The secondary structural elements are shown above the aligned sequences. Gray spheres represent disordered residues. Color-coding denotes sequence conservation among the proteins (white-to-green ramp, 30-100% identity). PMKSTRPN ( ), S. pneumoniae (strain R6) PMK; PMKSTRPY (GI:9937402), Streptococcus pyogenes PMK (Z-score = 2e-77; 50% identity); PMKENTFC (GI:9937388), Enterococcus faecalis PMK (Z-score = 2e-81; 29% identity); PMKLISIN (GI:16799091), putative Listeria innocua PMK (Z-score = 3e-68; 28% identity); PMKSTAHA (GI: 9937374), Staphylococcus haemolyticus PMK (Z-score = 8e-85; 29% identity); PMKSTAUR (GI: 9937366), S. aureus PMK (Z-score = 2e-84; 26% identity); MvKMETJA (GI: 15669275), M. jannaschii MK (Z-score = 1e-57; 21% identity), MvKENTFC (GI: 9937386), E. faecalis MK (Z-score = 6e-66; 18% identity).
Figure 2.
Figure 2. RIBBONS[15] drawing of PMK with labeled N- and C-termini and secondary structural elements color-coded for -helices (blue) and -strands (red). Motifs I, II, and III lining the putative active site cleft are shown in green.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2002, 47, 568-571) copyright 2002.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19509296 C.Fan, H.J.Fromm, and T.A.Bobik (2009).
Kinetic and functional analysis of L-threonine kinase, the PduX enzyme of Salmonella enterica.
  J Biol Chem, 284, 20240-20248.  
19485344 J.L.Andreassi, M.W.Vetting, P.W.Bilder, S.L.Roderick, and T.S.Leyh (2009).
Structure of the ternary complex of phosphomevalonate kinase: the enzyme and its family.
  Biochemistry, 48, 6461-6468.
PDB code: 3gon
18245852 C.Q.Diep, X.Tao, V.Pilauri, M.Losiewicz, T.E.Blank, and J.E.Hopper (2008).
Genetic evidence for sites of interaction between the Gal3 and Gal80 proteins of the Saccharomyces cerevisiae GAL gene switch.
  Genetics, 178, 725-736.  
17902708 T.J.Herdendorf, and H.M.Miziorko (2007).
Functional evaluation of conserved basic residues in human phosphomevalonate kinase.
  Biochemistry, 46, 11780-11788.  
17397541 T.Sgraja, T.K.Smith, and W.N.Hunter (2007).
Structure, substrate recognition and reactivity of Leishmania major mevalonate kinase.
  BMC Struct Biol, 7, 20.
PDB codes: 2hfs 2hfu
16219783 C.Q.Diep, G.Peng, M.Bewley, V.Pilauri, I.Ropson, and J.E.Hopper (2006).
Intragenic suppression of Gal3C interaction with Gal80 in the Saccharomyces cerevisiae GAL gene switch.
  Genetics, 172, 77-87.  
16006554 J.B.Thoden, and H.M.Holden (2005).
The molecular architecture of human N-acetylgalactosamine kinase.
  J Biol Chem, 280, 32784-32791.
PDB codes: 2a2c 2a2d
15632161 P.Acharya, M.Goenrich, C.H.Hagemeier, U.Demmer, J.A.Vorholt, R.K.Thauer, and U.Ermler (2005).
How an enzyme binds the C1 carrier tetrahydromethanopterin. Structure of the tetrahydromethanopterin-dependent formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1.
  J Biol Chem, 280, 13712-13719.
PDB codes: 1y5y 1y60
15802646 S.S.Doun, J.W.Burgner, S.D.Briggs, and V.W.Rodwell (2005).
Enterococcus faecalis phosphomevalonate kinase.
  Protein Sci, 14, 1134-1139.  
14767074 M.Hedl, and V.W.Rodwell (2004).
Enterococcus faecalis mevalonate kinase.
  Protein Sci, 13, 687-693.  
15229886 N.Fernandez-Fuentes, A.Hermoso, J.Espadaler, E.Querol, F.X.Aviles, and B.Oliva (2004).
Classification of common functional loops of kinase super-families.
  Proteins, 56, 539-555.  
14724278 S.C.Sinha, B.N.Chaudhuri, J.W.Burgner, G.Yakovleva, V.J.Davisson, and J.L.Smith (2004).
Crystal structure of imidazole glycerol-phosphate dehydratase: duplication of an unusual fold.
  J Biol Chem, 279, 15491-15498.
PDB code: 1rhy
12694189 D.J.Timson, and R.J.Reece (2003).
Functional analysis of disease-causing mutations in human galactokinase.
  Eur J Biochem, 270, 1767-1774.  
12424232 D.Pilloff, K.Dabovic, M.J.Romanowski, J.B.Bonanno, M.Doherty, S.K.Burley, and T.S.Leyh (2003).
The kinetic mechanism of phosphomevalonate kinase.
  J Biol Chem, 278, 4510-4515.  
12923184 H.M.Holden, I.Rayment, and J.B.Thoden (2003).
Structure and function of enzymes of the Leloir pathway for galactose metabolism.
  J Biol Chem, 278, 43885-43888.  
12796487 J.B.Thoden, and H.M.Holden (2003).
Molecular structure of galactokinase.
  J Biol Chem, 278, 33305-33311.
PDB code: 1pie
12672694 J.G.Luz, C.A.Hassig, C.Pickle, A.Godzik, B.J.Meyer, and I.A.Wilson (2003).
XOL-1, primary determinant of sexual fate in C. elegans, is a GHMP kinase family member and a structural prototype for a class of developmental regulators.
  Genes Dev, 17, 977-990.
PDB code: 1mg7
12878729 L.Miallau, M.S.Alphey, L.E.Kemp, G.A.Leonard, S.M.McSweeney, S.Hecht, A.Bacher, W.Eisenreich, F.Rohdich, and W.N.Hunter (2003).
Biosynthesis of isoprenoids: crystal structure of 4-diphosphocytidyl-2C-methyl-D-erythritol kinase.
  Proc Natl Acad Sci U S A, 100, 9173-9178.
PDB code: 1oj4
12771135 T.Wada, T.Kuzuyama, S.Satoh, S.Kuramitsu, S.Yokoyama, S.Unzai, J.R.Tame, and S.Y.Park (2003).
Crystal structure of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis.
  J Biol Chem, 278, 30022-30027.
PDB code: 1uek
12194989 S.K.Burley, and J.B.Bonanno (2002).
Structuring the universe of proteins.
  Annu Rev Genomics Hum Genet, 3, 243-262.  
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 code is shown on the right.