1N7M

Germline 7G12 with N-methylmesoporphyrin

Summary for 1N7M

• Entry DOI: 10.2210/pdb1n7m/pdb
• Related: 3FCT
• Descriptor: Germline Metal Chelatase Catalytic Antibody, chain H, Germline Metal Chelatase Catalytic Antibody, chain L, N-METHYLMESOPORPHYRIN, ... (4 entities in total)
• Functional Keywords: immune system
• Biological source: Mus musculus, Homo sapiens (house mouse, human); More
• Cellular location: Secreted: P01857
• Total number of polymer chains: 2
• Total formula weight: 46983.50

Authors

Yin, J.,Andryski, S.E.,Beuscher IV, A.E.,Stevens, R.C.,Schultz, P.G. (deposition date: 2002-11-15, release date: 2003-02-04, Last modification date: 2024-10-30)

Primary citation

Yin, J.,Andryski, S.E.,Beuscher IV, A.E.,Stevens, R.C.,Schultz, P.G.
Structural evidence for substrate strain in antibody catalysis
Proc.Natl.Acad.Sci.USA, 100:856-861, 2003

PubMed Abstract: The crystal structure of the Michaelis complex between the Fab fragment of ferrochelatase antibody 7G12 and its substrate mesoporphyrin has been solved to 2.6-A resolution. The antibody-bound mesoporphyrin clearly adopts a nonplanar conformation and reveals that the antibody catalyzes the porphyrin metallation reaction by straining/distorting the bound substrate toward the transition-state configuration. The crystal structures of the Fab fragment of the germ-line precursor antibody to 7G12 and its complex with the hapten N-methylmesoporphyrin have also been solved. A comparison of these structures with the corresponding structures of the affinity-matured antibody 7G12 reveals the molecular mechanism by which the immune system evolves binding energy to catalyze this reaction.

PubMed: 12552112
DOI: 10.1073/pnas.0235873100

Experimental method

X-RAY DIFFRACTION (1.8 Å)