2uyq: Difference between revisions
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==Overview== | ==Overview== | ||
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, .. | 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. | ||
==About this Structure== | ==About this Structure== | ||
2UYQ is a | 2UYQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_leprae Mycobacterium leprae] with SAM as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2UYQ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:41:50 2007'' | ||
