spacer
spacer

PDBsum entry 1ldx

Go to PDB code: 
protein links
Oxidoreductase, choh donor, NAD acceptr PDB id
1ldx
Jmol
Contents
Protein chain
330 a.a.
Superseded by: 2ldx
PDB id:
1ldx
Name: Oxidoreductase, choh donor, NAD acceptr
Structure: Lactate dehydrogenase isoenzyme c=4=
Source: Mouse (mus musculus) testicles, swiss- Webster strain
Authors: W.D.L.Musick,M.G.Rossmann
Key ref: W.D.Musick and M.G.Rossmann (1979). The structure of mouse testicular lactate dehydrogenase isoenzyme C4 at 2.9 A resolution. J Biol Chem, 254, 7611-7620. PubMed id: 468772
Date:
22-Sep-78     Release date:   13-Dec-78    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 329 a.a.
Key:    Secondary structure

 

 
J Biol Chem 254:7611-7620 (1979)
PubMed id: 468772  
 
 
The structure of mouse testicular lactate dehydrogenase isoenzyme C4 at 2.9 A resolution.
W.D.Musick, M.G.Rossmann.
 
  ABSTRACT  
 
The structure of lactate dehydrogenase isoenzyme C4 from mouse testes was solved at 2.9 A resolution using the technique of molecular replacement. The electron density map revealed a ternary-like configuration of the flexible loop peptide although density corresponding to the coenzyme and substrate molecules was not present. Apparently the apo-lactate dehydrogenase molecule in solution is in a dynamic equilibrium between the O (loop open as found in dogfish apo-lactate dehydrogenase M4) and C (loop closed as found in a variety of ternary complexes) conformations. During crystallization of the apoenzyme one or the other conformers is selected. The apparent stability of the closed conformation for the apo-lactate dehydrogenase C4 molecule may in part explain the low catalytic turnover number of the C isoenzyme. A possible substitution of an arginine residue at position 30 may also be a contributing factor as well as allowing NADP to act as coenzyme.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19875487 E.Goldberg, E.M.Eddy, C.Duan, and F.Odet (2010).
LDHC: the ultimate testis-specific gene.
  J Androl, 31, 86-94.  
17483170 J.R.Pineda, R.Callender, and S.D.Schwartz (2007).
Ligand binding and protein dynamics in lactate dehydrogenase.
  Biophys J, 93, 1474-1483.  
16632509 S.O.Yesylevskyy, V.N.Kharkyanen, and A.P.Demchenko (2006).
Dynamic protein domains: identification, interdependence, and stability.
  Biophys J, 91, 670-685.  
10089509 D.Rabinovich, H.Rozenberg, and Z.Shakked (1998).
Molecular replacement: the revival of the molecular Fourier transform method.
  Acta Crystallogr D Biol Crystallogr, 54, 1336-1342.  
7782128 N.Virji, and R.K.Naz (1995).
The role of lactate dehydrogenase-C4 in testicular function and infertility.
  Int J Androl, 18, 1-7.  
7534515 R.Sandulache, W.Pretsch, B.Chatterjee, W.Gimbel, J.Graw, and J.Favor (1994).
Molecular analysis of four lactate dehydrogenase-A mutants in the mouse.
  Mamm Genome, 5, 777-780.  
8479962 M.Michael, and G.Folkers (1993).
[Biological frost prevention in fish, frogs, flies and pines]
  Pharm Unserer Zeit, 22, 25-32.  
1620698 K.Huang, R.Kodandapani, H.Kallwass, J.K.Hogan, W.Parris, J.D.Friesen, M.Gold, J.B.Jones, and M.N.James (1992).
Crystallization and preliminary X-ray diffraction studies of two mutants of lactate dehydrogenase from Bacillus stearothermophilus.
  Proteins, 13, 158-161.  
2330370 K.Piontek, P.Chakrabarti, H.P.Schär, M.G.Rossmann, and H.Zuber (1990).
Structure determination and refinement of Bacillus stearothermophilus lactate dehydrogenase.
  Proteins, 7, 74-92.
PDB codes: 1ldb 2ldb
2160297 T.T.Tibbitts, D.L.Caspar, W.C.Phillips, and D.A.Goodenough (1990).
Diffraction diagnosis of protein folding in gap junction connexons.
  Biophys J, 57, 1025-1036.  
2440048 J.L.Millan, C.E.Driscoll, K.M.LeVan, and E.Goldberg (1987).
Epitopes of human testis-specific lactate dehydrogenase deduced from a cDNA sequence.
  Proc Natl Acad Sci U S A, 84, 5311-5315.  
2844458 Y.H.Edwards, S.Povey, K.M.LeVan, C.E.Driscoll, J.L.Millan, and E.Goldberg (1987).
Locus determining the human sperm-specific lactate dehydrogenase, LDHC, is syntenic with LDHA.
  Dev Genet, 8, 219-232.  
3794626 Z.G.Liang, J.A.Shelton, and E.Goldberg (1986).
Non-cross-reactivity of antibodies to murine LDH-C4 with LDH-A4 and LDH-B4.
  J Exp Zool, 240, 377-384.  
3886035 N.J.Leonard (1985).
Adenylates: bound and unbound.
  Biopolymers, 24, 9.  
3996406 S.S.Li, H.F.Tiano, K.M.Fukasawa, K.Yagi, M.Shimizu, F.S.Sharief, Y.Nakashima, and Y.E.Pan (1985).
Protein structure and gene organization of mouse lactate dehydrogenase-A isozyme.
  Eur J Biochem, 149, 215-225.  
6085454 T.E.Wheat, and E.Goldberg (1984).
Immunochemical dissection of the testes-specific isozyme lactate dehydrogenase C4.
  Ann N Y Acad Sci, 438, 156-170.  
6411472 R.Hensel, U.Mayr, and C.Woenckhaus (1983).
Affinity labelling of the allosteric site of the L-lactate dehydrogenase of Lactobacillus casei.
  Eur J Biochem, 135, 359-365.  
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.