1hm0: Difference between revisions

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[[Image:1hm0.gif|left|200px]]<br /><applet load="1hm0" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1hm0.gif|left|200px]]<br /><applet load="1hm0" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1hm0, resolution 2.3Å" />

'''CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE, GLMU'''<br />

==Overview==

The bifunctional bacterial enzyme N-acetyl-glucosamine-1-phosphate, uridyltransferase (GlmU) catalyzes the two-step formation of UDP-GlcNAc, a, fundamental precursor in bacterial cell wall biosynthesis. With the, emergence of new resistance mechanisms against beta-lactam and, glycopeptide antibiotics, the biosynthetic pathway of UDP-GlcNAc, represents an attractive target for drug design of new antibacterial, agents. The crystal structures of Streptococcus pneumoniae GlmU in unbound, form, in complex with acetyl-coenzyme A (AcCoA) and in complex with both, AcCoA and the end product UDP-GlcNAc, have been determined and refined to, 2.3, 2.5, and 1.75 A, respectively. The S. pneumoniae GlmU molecule is, organized in two separate domains connected via a long alpha-helical, linker and associates as a trimer, with the 50-A-long left-handed, beta-helix (LbetaH) C-terminal domains packed against each other in a, parallel fashion and the C-terminal region extended far away from the, LbetaH core and exchanged with the beta-helix from a neighboring subunit, in the trimer. AcCoA binding induces the formation of a long and narrow, tunnel, enclosed between two adjacent LbetaH domains and the interchanged, C-terminal region of the third subunit, giving rise to an original active, site architecture at the junction of three subunits.

The bifunctional bacterial enzyme N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU) catalyzes the two-step formation of UDP-GlcNAc, a fundamental precursor in bacterial cell wall biosynthesis. With the emergence of new resistance mechanisms against beta-lactam and glycopeptide antibiotics, the biosynthetic pathway of UDP-GlcNAc represents an attractive target for drug design of new antibacterial agents. The crystal structures of Streptococcus pneumoniae GlmU in unbound form, in complex with acetyl-coenzyme A (AcCoA) and in complex with both AcCoA and the end product UDP-GlcNAc, have been determined and refined to 2.3, 2.5, and 1.75 A, respectively. The S. pneumoniae GlmU molecule is organized in two separate domains connected via a long alpha-helical linker and associates as a trimer, with the 50-A-long left-handed beta-helix (LbetaH) C-terminal domains packed against each other in a parallel fashion and the C-terminal region extended far away from the LbetaH core and exchanged with the beta-helix from a neighboring subunit in the trimer. AcCoA binding induces the formation of a long and narrow tunnel, enclosed between two adjacent LbetaH domains and the interchanged C-terminal region of the third subunit, giving rise to an original active site architecture at the junction of three subunits.

==About this Structure==

1HM0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_diphosphorylase UDP-N-acetylglucosamine diphosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.23 2.7.7.23] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1HM0 OCA].

1HM0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_diphosphorylase UDP-N-acetylglucosamine diphosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.23 2.7.7.23] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HM0 OCA].

==Reference==

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[[Category: trimer]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 16~~:38:~~33 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:37 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1hm0.gif|left|200px]]<br /><applet load="1hm0" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1hm0.gif|left|200px]]<br /><applet load="1hm0" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1hm0, resolution 2.3&Aring;" />
 '''CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE, GLMU'''<br />
 ==Overview==
-The bifunctional bacterial enzyme N-acetyl-glucosamine-1-phosphate, uridyltransferase (GlmU) catalyzes the two-step formation of UDP-GlcNAc, a, fundamental precursor in bacterial cell wall biosynthesis. With the, emergence of new resistance mechanisms against beta-lactam and, glycopeptide antibiotics, the biosynthetic pathway of UDP-GlcNAc, represents an attractive target for drug design of new antibacterial, agents. The crystal structures of Streptococcus pneumoniae GlmU in unbound, form, in complex with acetyl-coenzyme A (AcCoA) and in complex with both, AcCoA and the end product UDP-GlcNAc, have been determined and refined to, 2.3, 2.5, and 1.75 A, respectively. The S. pneumoniae GlmU molecule is, organized in two separate domains connected via a long alpha-helical, linker and associates as a trimer, with the 50-A-long left-handed, beta-helix (LbetaH) C-terminal domains packed against each other in a, parallel fashion and the C-terminal region extended far away from the, LbetaH core and exchanged with the beta-helix from a neighboring subunit, in the trimer. AcCoA binding induces the formation of a long and narrow, tunnel, enclosed between two adjacent LbetaH domains and the interchanged, C-terminal region of the third subunit, giving rise to an original active, site architecture at the junction of three subunits.
+The bifunctional bacterial enzyme N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU) catalyzes the two-step formation of UDP-GlcNAc, a fundamental precursor in bacterial cell wall biosynthesis. With the emergence of new resistance mechanisms against beta-lactam and glycopeptide antibiotics, the biosynthetic pathway of UDP-GlcNAc represents an attractive target for drug design of new antibacterial agents. The crystal structures of Streptococcus pneumoniae GlmU in unbound form, in complex with acetyl-coenzyme A (AcCoA) and in complex with both AcCoA and the end product UDP-GlcNAc, have been determined and refined to 2.3, 2.5, and 1.75 A, respectively. The S. pneumoniae GlmU molecule is organized in two separate domains connected via a long alpha-helical linker and associates as a trimer, with the 50-A-long left-handed beta-helix (LbetaH) C-terminal domains packed against each other in a parallel fashion and the C-terminal region extended far away from the LbetaH core and exchanged with the beta-helix from a neighboring subunit in the trimer. AcCoA binding induces the formation of a long and narrow tunnel, enclosed between two adjacent LbetaH domains and the interchanged C-terminal region of the third subunit, giving rise to an original active site architecture at the junction of three subunits.
 ==About this Structure==
-HM0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_diphosphorylase UDP-N-acetylglucosamine diphosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.23 2.7.7.23] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HM0 OCA].
+HM0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_diphosphorylase UDP-N-acetylglucosamine diphosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.23 2.7.7.23] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HM0 OCA].
 ==Reference==
@@ Line 25: / Line 25: @@
 [[Category: trimer]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:38:33 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:37 2008''