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| {{STRUCTURE_2z9i| PDB=2z9i | SCENE= }} | | {{STRUCTURE_2z9i| PDB=2z9i | SCENE= }} |
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| '''Crystal structure of RV0983 from Mycobacterium tuberculosis- Proteolytically active form'''
| | ===Crystal structure of RV0983 from Mycobacterium tuberculosis- Proteolytically active form=== |
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| ==Overview==
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| The high-temperature requirement A (HtrA) family of serine proteases has been shown to play an important role in the environmental and cellular stress damage control system in Escherichia coli. Mycobacterium tuberculosis ( Mtb) has three putative HtrA-like proteases, HtrA1, HtrA2, and HtrA3. The deletion of htrA2 gives attenuated virulence in a mouse model of TB. Biochemical analysis reveals that HtrA2 can function both as a protease and as a chaperone. The three-dimensional structure of HtrA2 determined at 2.0 A resolution shows that the protease domains form the central core of the trimer and the PDZ domains extend to the periphery. Unlike E. coli DegS and DegP, the protease is naturally active due to the formation of the serine protease-like catalytic triad and its uniquely designed oxyanion hole. Both protease and PDZ binding pockets of each HtrA2 molecule are occupied by autoproteolytic peptide products and reveal clues for a novel autoregulatory mechanism that might have significant importance in HtrA-associated virulence of Mtb. | | The line below this paragraph, {{ABSTRACT_PUBMED_18479146}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18479146 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18479146}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| [[Category: Serine protease]] | | [[Category: Serine protease]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 10:46:02 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:28:40 2008'' |
