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1) Crystal structure of Bacillus subtilis Lon N-terminal domain

Duman, R.E.,   Lowe, J.

Journal: (2010) J.Mol.Biol. 401: 653-670 
PubMed: 20600124    
DOI: 10.1016/j.jmb.2010.06.030    
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PubMed Abstract:

Lon ATP-dependent proteases are key components of the protein quality control systems of bacterial cells and eukaryotic organelles. Eubacterial Lon proteases contain an N-terminal domain, an ATPase domain, and a protease domain, all in one polypeptide chain. The N-terminal domain is thought to be involved in substrate recognition, the ATPase domain in substrate unfolding and translocation into the protease chamber, and the protease domain in the hydrolysis of polypeptides into small peptide fragments.  Here, we present crystal structures of truncated versions of Lon protease from Bacillus subtilis (BsLon), which reveal previously unknown architectural features of Lon complexes. Our analytical ultracentrifugation and electron microscopy show different oligomerisation of Lon proteases from two different bacterial species, Aquifex aeolicus and B. subtilis.

Molecular Description

Classification	hydrolase
Structure Weight	48027.40
Molecule	ATP-dependent protease La 1
Polymer	1
Type	polypeptide(L)
Chains	A,B

2) Crystal Structure of Dipeptidyl Aminopeptidase IV from Stenotrophomonas maltophilia 

 


Dipeptidyl aminopeptidase IV from Stenotrophomonas maltophilia exhibits activity against a substrate containing a 4-hydroxyproline residue.

Journal: (2008) J.Bacteriol. 190: 7819-7829

PubMed: 18820015  
PubMedCentral: PMC2583625  
DOI: 10.1128/JB.02010-07  
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PubMed Abstract:

The crystal structure of dipeptidyl aminopeptidase IV from Stenotrophomonas maltophilia was determined at 2.8-A resolution by the multiple isomorphous replacement method, using platinum and selenomethionine derivatives. The crystals belong to space group P4(3)2(1)2, with unit cell parameters a = b... [ Read More & Search PubMed Abstracts ]

The crystal structure of dipeptidyl aminopeptidase IV from Stenotrophomonas maltophilia was determined at 2.8-A resolution by the multiple isomorphous replacement method, using platinum and selenomethionine derivatives. The crystals belong to space group P4(3)2(1)2, with unit cell parameters a = b = 105.9 A and c = 161.9 A. Dipeptidyl aminopeptidase IV is a homodimer, and the subunit structure is composed of two domains, namely, N-terminal beta-propeller and C-terminal catalytic domains. At the active site, a hydrophobic pocket to accommodate a proline residue of the substrate is conserved as well as those of mammalian enzymes. Stenotrophomonas dipeptidyl aminopeptidase IV exhibited activity toward a substrate containing a 4-hydroxyproline residue at the second position from the N terminus.One of the residues at the active sites is changed to Asn611. Accordingly, it was considered that Asn611 would be one of the major factors involved in the recognition of substrates containing 4-hydroxyproline.

Molecular Description

Classification	hydrolase
Structure Weight	82181.10
Molecule	Dipeptidyl peptidase IV
Polymer	1
Type	polypeptide(L)
Chains	A

3) Human START domain of Acyl-coenzyme A thioesterase 11 (ACOT1)

Journal : to be published

Molecular Description

Classification	lipid transport
Structure Weight	60191.69
Molecule	Thioesterase, adipose associated, isoform BFIT2
Polymer	1
Type	polypeptide(L)
Chains	A,B
Fragment	STARTdomain, UNP residues 339-594