Sandbox Reserved 110: Difference between revisions

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== Introduction ==

'''MraY''', called also '''phospho-N-acetylmuramoyl-pentapeptide-transferase''' or '''UDP-MurNAc-pentapeptide phosphotransferase''', with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.8.13 2.7.8.13], is an integral membrane enzyme involved in peptidoglycan biosynthesis <ref name="one">PMID:29778697</ref> <ref name="two">PMID:27511599</ref>.MraY is encoded by the mraY gene and belongs to a subfamily of the polyprenyl-phosphate N-acetyl hexosamine 1-phosphate transferase (PNPT) superfamily <ref name="three">PMID:23990562</ref>~~. MRAY is a promising candidate for the development of new antibiotics~~. MRAY is a promising candidate for the development of new antibiotics. In fact, it is the target of five classes of natural nucleoside inhibitors with potent antibacterial activity: the liposidomycins/caprazamycins, capuramycins, mureidomycins, muraymycins, and tunicamycins <ref name="two"/> <ref name="four">PMID:29438582</ref>.The structure presented in this page correspond to the MraY protein from ''Aquifex aeolicus'' (strain VF5), expressed in ''Escherichia coli'', in complex with carbacaprazamycin . '''Carbacaprazamycin''' is a chemically stable analog of caprazamycin nucleoside inhibitors <ref name="more1">DOI:10.1021/id5000376</ref>.

'''MraY''', called also '''phospho-N-acetylmuramoyl-pentapeptide-transferase''' or '''UDP-MurNAc-pentapeptide phosphotransferase''', with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.8.13 2.7.8.13], is an integral membrane enzyme involved in peptidoglycan biosynthesis <ref name="one">PMID:29778697</ref> <ref name="two">PMID:27511599</ref>.MraY is encoded by the mraY gene and belongs to a subfamily of the polyprenyl-phosphate N-acetyl hexosamine 1-phosphate transferase (PNPT) superfamily <ref name="three">PMID:23990562</ref>. MRAY is a promising candidate for the development of new antibiotics. In fact, it is the target of five classes of natural nucleoside inhibitors with potent antibacterial activity: the liposidomycins/caprazamycins, capuramycins, mureidomycins, muraymycins, and tunicamycins <ref name="two"/> <ref name="four">PMID:29438582</ref>.The structure presented in this page correspond to the MraY protein from ''Aquifex aeolicus'' (strain VF5), expressed in ''Escherichia coli'', in complex with carbacaprazamycin . '''Carbacaprazamycin''' is a chemically stable analog of caprazamycin nucleoside inhibitors <ref name="more1">DOI:10.1021/id5000376</ref>.

Drug resistant bacteria are the cause of death of millions of people worldwide. In the USA alone, hospital infections associated with antibiotic-resistant pathogens cause 99 000 deaths per year<ref name="more2">PMID:30349322</ref>. The development of new antibiotics with new mechanism of action is urgent. Structural analysis of the binding of carbacaprazamycin to MraY provides a better understanding of the chemical logic of MraY inhibition, which can help in the development of novel approaches for the design of antibiotics targeting MraY.

Sandbox Reserved 110: Difference between revisions

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 == Introduction ==
-'''MraY''', called also '''phospho-N-acetylmuramoyl-pentapeptide-transferase'''  or '''UDP-MurNAc-pentapeptide phosphotransferase''', with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.8.13 2.7.8.13], is an integral membrane enzyme involved in peptidoglycan biosynthesis <ref name="one">PMID:29778697</ref> <ref name="two">PMID:27511599</ref>.MraY is encoded by the mraY gene and   belongs to a subfamily of the polyprenyl-phosphate N-acetyl hexosamine 1-phosphate transferase (PNPT) superfamily <ref name="three">PMID:23990562</ref>. MRAY is a promising candidate for the development of new antibiotics. MRAY is a promising candidate for the development of new antibiotics. In fact, it is the target of five classes of natural nucleoside inhibitors with potent antibacterial activity: the liposidomycins/caprazamycins, capuramycins, mureidomycins, muraymycins, and tunicamycins <ref name="two"/> <ref name="four">PMID:29438582</ref>.The structure presented in this page correspond to the MraY protein from ''Aquifex aeolicus'' (strain VF5), expressed in ''Escherichia coli'', in complex with carbacaprazamycin . '''Carbacaprazamycin''' is a chemically stable analog of caprazamycin nucleoside inhibitors <ref name="more1">DOI:10.1021/id5000376</ref>.
+'''MraY''', called also '''phospho-N-acetylmuramoyl-pentapeptide-transferase'''  or '''UDP-MurNAc-pentapeptide phosphotransferase''', with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.8.13 2.7.8.13], is an integral membrane enzyme involved in peptidoglycan biosynthesis <ref name="one">PMID:29778697</ref> <ref name="two">PMID:27511599</ref>.MraY is encoded by the mraY gene and   belongs to a subfamily of the polyprenyl-phosphate N-acetyl hexosamine 1-phosphate transferase (PNPT) superfamily <ref name="three">PMID:23990562</ref>. MRAY is a promising candidate for the development of new antibiotics. In fact, it is the target of five classes of natural nucleoside inhibitors with potent antibacterial activity: the liposidomycins/caprazamycins, capuramycins, mureidomycins, muraymycins, and tunicamycins <ref name="two"/> <ref name="four">PMID:29438582</ref>.The structure presented in this page correspond to the MraY protein from ''Aquifex aeolicus'' (strain VF5), expressed in ''Escherichia coli'', in complex with carbacaprazamycin . '''Carbacaprazamycin''' is a chemically stable analog of caprazamycin nucleoside inhibitors <ref name="more1">DOI:10.1021/id5000376</ref>.
 Drug resistant bacteria are the cause of death of millions of people worldwide. In the USA alone, hospital infections associated with antibiotic-resistant pathogens cause 99 000 deaths per year<ref name="more2">PMID:30349322</ref>. The development of new antibiotics with new mechanism of action is urgent. Structural analysis of the binding of carbacaprazamycin to MraY provides a better understanding of the chemical logic of MraY inhibition, which can help in the development of novel approaches for the design of antibiotics targeting MraY.