1hv9
From Proteopedia
(New page: 200px<br /><applet load="1hv9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hv9, resolution 2.10Å" /> '''STRUCTURE OF E. COLI...) |
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| - | [[Image:1hv9.jpg|left|200px]]<br /><applet load="1hv9" size=" | + | [[Image:1hv9.jpg|left|200px]]<br /><applet load="1hv9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hv9, resolution 2.10Å" /> | caption="1hv9, resolution 2.10Å" /> | ||
'''STRUCTURE OF E. COLI GLMU: ANALYSIS OF PYROPHOSPHORYLASE AND ACETYLTRANSFERASE ACTIVE SITES'''<br /> | '''STRUCTURE OF E. COLI GLMU: ANALYSIS OF PYROPHOSPHORYLASE AND ACETYLTRANSFERASE ACTIVE SITES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | N-Acetylglucosamine-1-PO(4) uridyltransferase (GlmU) is a trimeric | + | N-Acetylglucosamine-1-PO(4) uridyltransferase (GlmU) is a trimeric bifunctional enzyme that catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-GlcNAc. The X-ray crystal structure of Escherichia coli GlmU in complex with UDP-GlcNAc and CoA has been determined to 2.1 A resolution and reveals a two-domain architecture that is responsible for these two reactions. The C-terminal domain is responsible for the CoA-dependent acetylation of Glc-1-PO(4) to GlcNAc-1-PO(4) and displays the longest left-handed parallel beta-helix observed to date. The acetyltransferase active site defined by the binding site for CoA makes use of residues from all three subunits and is positioned beneath an open cavity large enough to accommodate the Glc-1-PO(4) acetyl acceptor. The N-terminal domain catalyzes uridyl transfer from UTP to GlcNAc-1-PO(4) to form the final products UDP-GlcNAc and pyrophosphate. This domain is composed of a central seven-stranded beta-sheet surrounded by six alpha-helices in a Rossmann fold-like topology. A Co(2+) ion binds to just one of the two independent pyrophosphorylase active sites present in the crystals studied here, each of which nonetheless binds UDP-GlcNAc. The conformational changes of the enzyme and sugar nucleotide that accompany metal binding may provide a window into the structural dynamics that accompany catalysis. |
==About this Structure== | ==About this Structure== | ||
| - | 1HV9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CO, COA and UD1 as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 1HV9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CO:'>CO</scene>, <scene name='pdbligand=COA:'>COA</scene> and <scene name='pdbligand=UD1:'>UD1</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1HV9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: UDP-N-acetylglucosamine diphosphorylase]] | [[Category: UDP-N-acetylglucosamine diphosphorylase]] | ||
| - | [[Category: Olsen, L | + | [[Category: Olsen, L R.]] |
| - | [[Category: Roderick, S | + | [[Category: Roderick, S L.]] |
[[Category: CO]] | [[Category: CO]] | ||
[[Category: COA]] | [[Category: COA]] | ||
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[[Category: left-handed parallel beta-helix]] | [[Category: left-handed parallel beta-helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:05:11 2008'' |
Revision as of 11:05, 21 February 2008
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STRUCTURE OF E. COLI GLMU: ANALYSIS OF PYROPHOSPHORYLASE AND ACETYLTRANSFERASE ACTIVE SITES
Overview
N-Acetylglucosamine-1-PO(4) uridyltransferase (GlmU) is a trimeric bifunctional enzyme that catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-GlcNAc. The X-ray crystal structure of Escherichia coli GlmU in complex with UDP-GlcNAc and CoA has been determined to 2.1 A resolution and reveals a two-domain architecture that is responsible for these two reactions. The C-terminal domain is responsible for the CoA-dependent acetylation of Glc-1-PO(4) to GlcNAc-1-PO(4) and displays the longest left-handed parallel beta-helix observed to date. The acetyltransferase active site defined by the binding site for CoA makes use of residues from all three subunits and is positioned beneath an open cavity large enough to accommodate the Glc-1-PO(4) acetyl acceptor. The N-terminal domain catalyzes uridyl transfer from UTP to GlcNAc-1-PO(4) to form the final products UDP-GlcNAc and pyrophosphate. This domain is composed of a central seven-stranded beta-sheet surrounded by six alpha-helices in a Rossmann fold-like topology. A Co(2+) ion binds to just one of the two independent pyrophosphorylase active sites present in the crystals studied here, each of which nonetheless binds UDP-GlcNAc. The conformational changes of the enzyme and sugar nucleotide that accompany metal binding may provide a window into the structural dynamics that accompany catalysis.
About this Structure
1HV9 is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as UDP-N-acetylglucosamine diphosphorylase, with EC number 2.7.7.23 Full crystallographic information is available from OCA.
Reference
Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites., Olsen LR, Roderick SL, Biochemistry. 2001 Feb 20;40(7):1913-21. PMID:11329257
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