1YEH

STRUCTURE OF IGG2A FAB FRAGMENT

Summary for 1YEH

• Entry DOI: 10.2210/pdb1yeh/pdb
• Descriptor: FAB FRAGMENT, ZINC ION, ... (4 entities in total)
• Functional Keywords: catalytic antibody, immunoglobulin c region
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 48652.90

Authors

Gigant, B.,Knossow, M. (deposition date: 1997-05-29, release date: 1997-12-03, Last modification date: 2024-10-30)

Primary citation

Gigant, B.,Charbonnier, J.B.,Eshhar, Z.,Green, B.S.,Knossow, M.
X-ray structures of a hydrolytic antibody and of complexes elucidate catalytic pathway from substrate binding and transition state stabilization through water attack and product release.
Proc.Natl.Acad.Sci.USA, 94:7857-7861, 1997

PubMed Abstract: The x-ray structures of the unliganded esterase-like catalytic antibody D2.3 and its complexes with a substrate analogue and with one of the reaction products are analyzed. Together with the structure of the phosphonate transition state analogue hapten complex, these crystal structures provide a complete description of the reaction pathway. At alkaline pH, D2.3 acts by preferential stabilization of the negatively charged oxyanion intermediate of the reaction that results from hydroxide attack on the substrate. A tyrosine residue plays a crucial role in catalysis: it activates the ester substrate and, together with an asparagine, it stabilizes the oxyanion intermediate. A canal allows facile diffusion of water molecules to the reaction center that is deeply buried in the structure. Residues bordering this canal provide targets for mutagenesis to introduce a general base in the vicinity of the reaction center.

PubMed: 9223277
DOI: 10.1073/pnas.94.15.7857

Experimental method

X-RAY DIFFRACTION (2.55 Å)