1zps: Difference between revisions
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'''Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI''' | {{Structure | ||
|PDB= 1zps |SIZE=350|CAPTION= <scene name='initialview01'>1zps</scene>, resolution 1.7Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoribosyl-AMP_cyclohydrolase Phosphoribosyl-AMP cyclohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.19 3.5.4.19] | |||
|GENE= hisI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=145262 Methanothermobacter thermautotrophicus]) | |||
}} | |||
'''Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ZPS is a [ | 1ZPS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZPS OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI., Sivaraman J, Myers RS, Boju L, Sulea T, Cygler M, Jo Davisson V, Schrag JD, Biochemistry. 2005 Aug 2;44(30):10071-80. PMID:[http:// | Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI., Sivaraman J, Myers RS, Boju L, Sulea T, Cygler M, Jo Davisson V, Schrag JD, Biochemistry. 2005 Aug 2;44(30):10071-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16042384 16042384] | ||
[[Category: Methanothermobacter thermautotrophicus]] | [[Category: Methanothermobacter thermautotrophicus]] | ||
[[Category: Phosphoribosyl-AMP cyclohydrolase]] | [[Category: Phosphoribosyl-AMP cyclohydrolase]] | ||
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[[Category: histidine biosynthesis]] | [[Category: histidine biosynthesis]] | ||
[[Category: montreal-kingston bacterial structural genomics initiative]] | [[Category: montreal-kingston bacterial structural genomics initiative]] | ||
[[Category: structural | [[Category: structural genomic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:38:23 2008'' | ||
Revision as of 16:38, 20 March 2008
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| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | hisI (Methanothermobacter thermautotrophicus) | ||||||
| Activity: | Phosphoribosyl-AMP cyclohydrolase, with EC number 3.5.4.19 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI
OverviewOverview
The metabolic pathway for histidine biosynthesis is interesting from an evolutionary perspective because of the diversity of gene organizations and protein structures involved. Hydrolysis of phosphoribosyl-AMP, the third step in the histidine biosynthetic pathway, is carried out by PR-AMP cyclohydrolase, the product of the hisI gene. The three-dimensional structure of PR-AMP cyclohydrolase from Methanobacterium thermoautotrophicum was solved and refined to 1.7 A resolution. The enzyme is a homodimer. The position of the Zn(2+)-binding site that is essential for catalysis was inferred from the positions of bound Cd(2+) ions, which were part of the crystallization medium. These metal binding sites include three cysteine ligands, two from one monomer and the third from the second monomer. The enzyme remains active when Cd(2+) is substituted for Zn(2+). The likely binding site for Mg(2+), also necessary for activity in a homologous cyclohydrolase, was also inferred from Cd(2+) positions and is comprised of aspartic acid side chains. The putative substrate-binding cleft is formed at the interface between the two monomers of the dimer. This fact, combined with the localization of the Zn(2+)-binding site, indicates that the enzyme is an obligate dimer.
About this StructureAbout this Structure
1ZPS is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI., Sivaraman J, Myers RS, Boju L, Sulea T, Cygler M, Jo Davisson V, Schrag JD, Biochemistry. 2005 Aug 2;44(30):10071-80. PMID:16042384
Page seeded by OCA on Thu Mar 20 15:38:23 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Methanothermobacter thermautotrophicus
- Phosphoribosyl-AMP cyclohydrolase
- Single protein
- BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.
- Boju, L.
- Cygler, M.
- Davisson, V J.
- Myers, R S.
- Schrag, J D.
- Sivaraman, J.
- Sulea, T.
- ACY
- CD
- Bsgi
- Histidine biosynthesis
- Montreal-kingston bacterial structural genomics initiative
- Structural genomic