1hm0

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[[Image:1hm0.gif|left|200px]]<br /><applet load="1hm0" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1hm0.gif|left|200px]]
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caption="1hm0, resolution 2.3&Aring;" />
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'''CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE, GLMU'''<br />
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{{Structure
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|PDB= 1hm0 |SIZE=350|CAPTION= <scene name='initialview01'>1hm0</scene>, resolution 2.3&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY= [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]
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|GENE= GLMU ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 Streptococcus pneumoniae])
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}}
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'''CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE, GLMU'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1HM0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HM0 OCA].
==Reference==
==Reference==
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Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture., Sulzenbacher G, Gal L, Peneff C, Fassy F, Bourne Y, J Biol Chem. 2001 Apr 13;276(15):11844-51. Epub 2000 Dec 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11118459 11118459]
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Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture., Sulzenbacher G, Gal L, Peneff C, Fassy F, Bourne Y, J Biol Chem. 2001 Apr 13;276(15):11844-51. Epub 2000 Dec 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11118459 11118459]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streptococcus pneumoniae]]
[[Category: Streptococcus pneumoniae]]
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[[Category: trimer]]
[[Category: trimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:38:49 2008''

Revision as of 09:38, 20 March 2008


PDB ID 1hm0

Drag the structure with the mouse to rotate
, resolution 2.3Å
Ligands:
Gene: GLMU (Streptococcus pneumoniae)
Activity: UDP-N-acetylglucosamine diphosphorylase, with EC number 2.7.7.23
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF S.PNEUMONIAE N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE, GLMU


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.

About this Structure

1HM0 is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.

Reference

Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture., Sulzenbacher G, Gal L, Peneff C, Fassy F, Bourne Y, J Biol Chem. 2001 Apr 13;276(15):11844-51. Epub 2000 Dec 15. PMID:11118459

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