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| - | [[Image:2ckd.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2ckd| PDB=2ckd | SCENE= }} | | {{STRUCTURE_2ckd| PDB=2ckd | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF ML2640 FROM MYCOBACTERIUM LEPRAE'''
| + | ===CRYSTAL STRUCTURE OF ML2640 FROM MYCOBACTERIUM LEPRAE=== |
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| - | ==Overview==
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| - | Mycobacterium leprae protein ML2640c belongs to a large family of conserved hypothetical proteins predominantly found in mycobacteria, some of them predicted as putative S-adenosylmethionine (AdoMet)-dependent methyltransferases (MTase). As part of a Structural Genomics initiative on conserved hypothetical proteins in pathogenic mycobacteria, we have determined the structure of ML2640c in two distinct crystal forms. As expected, ML2640c has a typical MTase core domain and binds the methyl donor substrate AdoMet in a manner consistent with other known members of this structural family. The putative acceptor substrate-binding site of ML2640c is a large internal cavity, mostly lined by aromatic and aliphatic side-chain residues, suggesting that a lipid-like molecule might be targeted for catalysis. A flap segment (residues 222-256), which isolates the binding site from the bulk solvent and is highly mobile in the crystal structures, could serve as a gateway to allow substrate entry and product release. The multiple sequence alignment of ML2640c-like proteins revealed that the central alpha/beta core and the AdoMet-binding site are very well conserved within the family. However, the amino acid positions defining the binding site for the acceptor substrate display a higher variability, suggestive of distinct acceptor substrate specificities. The ML2640c crystal structures offer the first structural glimpses at this important family of mycobacterial proteins and lend strong support to their functional assignment as AdoMet-dependent methyltransferases.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17660248}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17660248 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17660248}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hypothetical protein]] | | [[Category: Hypothetical protein]] |
| | [[Category: Transferase]] | | [[Category: Transferase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:20:57 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:12:43 2008'' |
Revision as of 07:12, 29 July 2008
Template:STRUCTURE 2ckd
CRYSTAL STRUCTURE OF ML2640 FROM MYCOBACTERIUM LEPRAE
Template:ABSTRACT PUBMED 17660248
About this Structure
2CKD is a Single protein structure of sequence from Mycobacterium leprae. Full crystallographic information is available from OCA.
Reference
The crystal structure of M. leprae ML2640c defines a large family of putative S-adenosylmethionine-dependent methyltransferases in mycobacteria., Grana M, Haouz A, Buschiazzo A, Miras I, Wehenkel A, Bondet V, Shepard W, Schaeffer F, Cole ST, Alzari PM, Protein Sci. 2007 Sep;16(9):1896-904. Epub 2007 Jul 27. PMID:17660248
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