STRUCTURE 1BM0

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spinqualitylabelsall models PDB ID 1bm0 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1bm0, resolution 2.50Å ()
Structural annotation: Resources: CATH : 1Bm0A03, 1Bm0A06, 1Bm0A05, 1Bm0A02, 1Bm0A04, 1Bm0A01, 1Bm0B01, 1Bm0B02, 1Bm0B04, 1Bm0B05, 1Bm0B06, 1Bm0B03 InterPro : Ipr000264, Ipr001703, Ipr014760 Pfam : PF00273 SCOP : d1bm0a3, d1bm0a2, d1bm0a1, d1bm0b2, d1bm0b3, d1bm0b1 UniProt : P02768
Functional annotation: Cellular component: extracellular region extracellular space protein complex Biological process: hemolysis by symbiont of host red blood cells maintenance of mitochondrion localization negative regulation of apoptosis cellular response to starvation negative regulation of non-apoptotic programmed cell death transport Molecular function: DNA binding antioxidant activity protein binding copper ion binding toxin binding pyridoxal phosphate binding drug binding oxygen binding metal ion binding lipid binding fatty acid binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Contents 1 Abstract 2 Introduction 3 Crystallization of the tetragonal crystal 4 crystallization of the triclinic crystal 5 structural determination of the triclinic crystal 6 Results 6.1 Structural determination and quality 6.2 Local symmetry in the triclinic lattice 6.3 Overall structure 6.4 Subdomains 6.5 Free sulfhydryl group at cys34 6.6 Binding sites for drugs and other compounds 7 Conclusion 8 References

Abstract

The three dimensional structures of pHSA and rHSA triclinic crystals were determined at 2.5A°resolution through multiple isomorphous replacement with a known tetragonal crystal. The pHSA and rHSA structures are similar with an r.m.s deviation of 0.24 A° for all the cα atoms. Cys 34 does not have a disulfide link with any ligand. A pocket of hydrophobic and positively charged residues is formed at domains 2 and 3 where a wide range of compounds can be accommodated. The surface of the domain has three binding sites for long chain fatty acids.

Introduction

HSA has a blood concentration of 5g/100ml and is the most abundant protein in the blood plasma. HSA has a high affinity for cu+2, zn+2, fatty acids , amino acids , metabolites and many other drug compounds. The protein brings solutes in the blood to the target organs and also maintains the PH and osmotic pressure of the plasma hence it is used as a carrier of drugs to their targets. HSA has 585 residues with 17 disulfide bridges and one free cysteine. Many reports contained crystal forms of HSA but none provided structural information. This article discusses the crystal form of defatted HSA and the molecular aspects of the protein are determined at the highest resolution.

Crystallization of the tetragonal crystal

crystallization of the triclinic crystal

structural determination of the triclinic crystal

Results

Structural determination and quality

Local symmetry in the triclinic lattice

Overall structure

Subdomains

Free sulfhydryl group at cys34

Binding sites for drugs and other compounds

Conclusion

References