1zps: Difference between revisions

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<StructureSection load='1zps' size='340' side='right'caption='[[1zps]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1zps' size='340' side='right'caption='[[1zps]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1zps]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"methanobacterium_thermoautotrophicus"_(sic)_zeikus_and_wolfe_1972 "methanobacterium thermoautotrophicus" (sic) zeikus and wolfe 1972]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZPS FirstGlance]. <br>
<table><tr><td colspan='2'>[[1zps]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZPS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hisI ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=145262 "Methanobacterium thermoautotrophicus" (sic) Zeikus and Wolfe 1972])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoribosyl-AMP_cyclohydrolase Phosphoribosyl-AMP cyclohydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.19 3.5.4.19] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zps OCA], [https://pdbe.org/1zps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zps RCSB], [https://www.ebi.ac.uk/pdbsum/1zps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zps ProSAT], [https://www.topsan.org/Proteins/BSGI/1zps TOPSAN]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zps OCA], [https://pdbe.org/1zps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zps RCSB], [https://www.ebi.ac.uk/pdbsum/1zps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zps ProSAT], [https://www.topsan.org/Proteins/BSGI/1zps TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/HIS3_METTH HIS3_METTH]] Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.  
[https://www.uniprot.org/uniprot/HIS3_METTH HIS3_METTH] Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zps ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zps ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:16042384</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1zps" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cyclohydrolase 3D structures|Cyclohydrolase 3D structures]]
*[[Cyclohydrolase 3D structures|Cyclohydrolase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Phosphoribosyl-AMP cyclohydrolase]]
[[Category: Methanothermobacter thermautotrophicus]]
[[Category: Structural genomic]]
[[Category: Boju L]]
[[Category: Boju, L]]
[[Category: Cygler M]]
[[Category: Cygler, M]]
[[Category: Davisson VJ]]
[[Category: Davisson, V J]]
[[Category: Myers RS]]
[[Category: Myers, R S]]
[[Category: Schrag JD]]
[[Category: Schrag, J D]]
[[Category: Sivaraman J]]
[[Category: Sivaraman, J]]
[[Category: Sulea T]]
[[Category: Sulea, T]]
[[Category: Bsgi]]
[[Category: Histidine biosynthesis]]
[[Category: Hydrolase]]

Latest revision as of 12:06, 14 February 2024

Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisICrystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI

Structural highlights

1zps is a 2 chain structure with sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

HIS3_METTH Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1zps, resolution 1.70Å

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