50,000!

From PDBWiki

On the 8th of April 2008, the number of macromolecular structures released into the PDB reached 50,000. This milestone in structural biology represents over half a century of technological, scientific and cultural progress.

For structural biologists, this landmark event represents the pinnacle of human scientific achievement, encompassing countless innovations, discoveries and scientific breakthroughs.

The very first protein structures were solved in 1960 showing for the first time the atomic coordinates of horse hemoglobin and sperm whale myoglobin (Perutz 1960, Kendrew 1960). These initial structures provided a wealth of data for the analysis of proteins and generated tens of scientific publications. These early structures served both as a means of validating previous theoretical models (Pauling 1951a, Pauling 1951b, Kauzmann 1959) and as a basis for developing new theories of protein structure, function and evolution (Perutz 1962, Monod 1965, Perutz 1965).

For example, the structure of myoglobin confirmed the model of alpha-helix proposed by Pauling. Despite the different amino acid composition of hemoglobin, the structure of its subunits showed essentially the same tertiary structure as myoglobin. At the time this observation lead Kendrew to comment that "myoglobin possesses a structure the significance of which extends beyond a particular species and even beyond a particular protein".

Today these facts are taken for granted.

[edit] External links

PDB Archive Contains More Than 50,000 Structures

[edit] References

Perutz 1960 

Perutz, M F and Rossmann, M G and Cullis, A F and Muirhead, H and Will, G and North, A C T. Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5 Angstrom resolution, obtained by X-ray analysis. Nature. 185:416-22. 1960.

Kendrew 1960 

Kendrew, J C and Dickerson, R E and Strandberg, B E and Hart, R G and Davies, R D and Phillips, D C and Shore, V C. Structure of myoglobin: a three-dimensional Fourier synthesis at 2.0 Angstroms resolution. Nature. 185:422-427. 1960.

Pauling 1951a 

Pauling, L And Corey, R B And Branson, H R. The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain. PNAS. 37(4):205-211. 1951. PMID 14816373.

Puling 1951b 

Pauling, L And Corey, R B. The pleated sheet, a new layer configuration of polypeptide chains. PNAS. 37(5):251-256. 1951. PMID 14834147.

Kauzmann 1959 

Kauzmann, W. Some factors in the interpretation of protein denaturation. Adv Protein Chem. 14:1-63. 1959. PMID 14404936.

Perutz 1962 

Perutz, M F. Relation between structure and sequence of haemoglobin. Nature. 194:914-917. 1962. PMID 14485628.

Monod 1965 

Monod, J And Wyman, J And Changeux, J P. On the nature of allosteric transitions: A plausible model. JMB. 12:88-118. PMID 14343300.

Perutz 1965 

Perutz, M F and Kendrew, J C and Watson H C. Structure and function of haemoglobin II. Some relations between polypeptide chain configuration and amino acid sequence. JMB. 13:669-678. 1965.