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2ntm

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[[Image:2ntm.gif|left|200px]]
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{{STRUCTURE_2ntm| PDB=2ntm | SCENE= }}
{{STRUCTURE_2ntm| PDB=2ntm | SCENE= }}
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'''Crystal structure of PurO from Methanothermobacter thermoautotrophicus'''
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===Crystal structure of PurO from Methanothermobacter thermoautotrophicus===
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==Overview==
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Inosine 5'-monophosphate (IMP) cyclohydrolase catalyzes the cyclization of 5-formaminoimidazole-4-carboxamide ribonucleotide (FAICAR) to IMP in the final step of de novo purine biosynthesis. Two major types of this enzyme have been discovered to date: PurH in Bacteria and Eukarya and PurO in Archaea. The structure of the MTH1020 gene product from Methanothermobacter thermoautotrophicus was previously solved without functional annotation but shows high amino acid sequence similarity to other PurOs. We determined the crystal structure of the MTH1020 gene product in complex with either IMP or 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) at 2.0 and 2.6 A resolution, respectively. On the basis of the sequence analysis, ligand-bound structures, and biochemical data, MTH1020 is confirmed as an archaeal IMP cyclohydrolase, thus designated as MthPurO. MthPurO has a four-layered alphabeta betaalpha core structure, showing an N-terminal nucleophile (NTN) hydrolase fold. The active site is located at the deep pocket between two central beta-sheets and contains residues strictly conserved within PurOs. Comparisons of the two types of IMP cyclohydrolase, PurO and PurH, revealed that there are no similarities in sequence, structure, or the active site architecture, suggesting that they are evolutionarily not related to each other. The MjR31K mutant of PurO from Methanocaldococcus jannaschii showed 76% decreased activity and the MjE102Q mutation completely abolished enzymatic activity, suggesting that these highly conserved residues play critical roles in catalysis. Interestingly, green fluorescent protein (GFP), which has no structural homology to either PurO or PurH but catalyzes a similar intramolecular cyclohydrolase reaction required for chromophore maturation, utilizes Arg96 and Glu222 in a mechanism analogous to that of PurO.
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{{ABSTRACT_PUBMED_17407260}}
==About this Structure==
==About this Structure==
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[[Category: White, R H.]]
[[Category: White, R H.]]
[[Category: Alpha-beta-beta-alpha ntn hydrolase fold]]
[[Category: Alpha-beta-beta-alpha ntn hydrolase fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:53:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:43:58 2008''

Revision as of 14:44, 28 July 2008

Image:2ntm.png

Template:STRUCTURE 2ntm

Crystal structure of PurO from Methanothermobacter thermoautotrophicus

Template:ABSTRACT PUBMED 17407260

About this Structure

2NTM is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.

Reference

A novel function for the N-terminal nucleophile hydrolase fold demonstrated by the structure of an archaeal inosine monophosphate cyclohydrolase., Kang YN, Tran A, White RH, Ealick SE, Biochemistry. 2007 May 1;46(17):5050-62. Epub 2007 Apr 4. PMID:17407260

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