1h1c: Difference between revisions

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[[Image:1h1c.gif|left|200px]]


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==Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima==
The line below this paragraph, containing "STRUCTURE_1h1c", creates the "Structure Box" on the page.
<StructureSection load='1h1c' size='340' side='right'caption='[[1h1c]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1h1c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H1C FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
{{STRUCTURE_1h1c|  PDB=1h1c |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h1c OCA], [https://pdbe.org/1h1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h1c RCSB], [https://www.ebi.ac.uk/pdbsum/1h1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h1c ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HIS8_THEMA HIS8_THEMA]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h1/1h1c_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1h1c ConSurf].
<div style="clear:both"></div>


'''HISTIDINOL-PHOSPHATE AMINOTRANSFERASE (HISC) FROM THERMOTOGA MARITIMA'''
==See Also==
 
*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
In histidine biosynthesis, histidinol-phosphate aminotransferase catalyzes the transfer of the amino group from glutamate to imidazole acetol-phosphate producing 2-oxoglutarate and histidinol phosphate. In some organisms such as the hyperthermophile Thermotoga maritima, specific tyrosine and aromatic amino acid transaminases have not been identified to date, suggesting an additional role for histidinol-phosphate aminotransferase in other transamination reactions generating aromatic amino acids. To gain insight into the specific function of this transaminase, we have determined its crystal structure in the absence of any ligand except phosphate, in the presence of covalently bound pyridoxal 5'-phosphate, of the coenzyme histidinol phosphate adduct, and of pyridoxamine 5'-phosphate. The enzyme accepts histidinol phosphate, tyrosine, tryptophan, and phenylalanine, but not histidine, as substrates. The structures provide a model of how these different substrates could be accommodated by histidinol-phosphate aminotransferase. Some of the structural features of the enzyme are more preserved between the T. maritima enzyme and a related threonine-phosphate decarboxylase from S. typhimurium than with histidinol-phosphate aminotransferases from different organisms.
[[Category: Large Structures]]
 
==About this Structure==
1H1C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1C OCA].
 
==Reference==
Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase., Fernandez FJ, Vega MC, Lehmann F, Sandmeier E, Gehring H, Christen P, Wilmanns M, J Biol Chem. 2004 May 14;279(20):21478-88. Epub 2004 Mar 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15007066 15007066]
[[Category: Histidinol-phosphate transaminase]]
[[Category: Single protein]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Fernandez, F J.]]
[[Category: Fernandez FJ]]
[[Category: Vega, M C.]]
[[Category: Vega MC]]
[[Category: Wilmanns, M.]]
[[Category: Wilmanns M]]
[[Category: Aminotransferase]]
[[Category: Histidine biosynthesis]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:17:39 2008''

Latest revision as of 14:26, 27 March 2024

Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritimaHistidinol-phosphate aminotransferase (HisC) from Thermotoga maritima

Structural highlights

1h1c is a 4 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.85Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HIS8_THEMA

Evolutionary Conservation

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

See Also

1h1c, resolution 2.85Å

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