3c9q: Difference between revisions

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[[Image:3c9q.jpg|left|200px]]


{{Structure
==Crystal structure of the uncharacterized human protein C8orf32 with bound peptide==
|PDB= 3c9q |SIZE=350|CAPTION= <scene name='initialview01'>3c9q</scene>, resolution 1.50&Aring;
<StructureSection load='3c9q' size='340' side='right'caption='[[3c9q]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+A+206'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Residue+A+207'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Residue+A+208'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Residue+A+209'>AC4</scene>, <scene name='pdbsite=AC5:So4+Binding+Site+For+Residue+A+210'>AC5</scene>, <scene name='pdbsite=AC6:Co3+Binding+Site+For+Residue+A+211'>AC6</scene>, <scene name='pdbsite=AC7:Edo+Binding+Site+For+Residue+A+212'>AC7</scene>, <scene name='pdbsite=AC8:Edo+Binding+Site+For+Residue+A+213'>AC8</scene>, <scene name='pdbsite=AC9:Edo+Binding+Site+For+Residue+A+214'>AC9</scene>, <scene name='pdbsite=BC1:Edo+Binding+Site+For+Residue+A+215'>BC1</scene> and <scene name='pdbsite=BC2:Edo+Binding+Site+For+Residue+A+216'>BC2</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
<table><tr><td colspan='2'>[[3c9q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C9Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C9Q FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
|GENE= C8orf32 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3c9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c9q OCA], [https://pdbe.org/3c9q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c9q RCSB], [https://www.ebi.ac.uk/pdbsum/3c9q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c9q ProSAT], [https://www.topsan.org/Proteins/CESG/3c9q TOPSAN]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c9q OCA], [http://www.ebi.ac.uk/pdbsum/3c9q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3c9q RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/NTAQ1_HUMAN NTAQ1_HUMAN] Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine (By similarity).
 
== Evolutionary Conservation ==
'''Crystal structure of the uncharacterized human protein C8orf32 with bound peptide'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/3c9q_consurf.spt"</scriptWhenChecked>
3C9Q is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C9Q OCA].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3c9q ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Bingman, C A.]]
[[Category: Bingman CA]]
[[Category: Bitto, E.]]
[[Category: Bitto E]]
[[Category: CESG, Center for Eukaryotic Structural Genomics.]]
[[Category: McCoy JG]]
[[Category: Jr., G N.Phillips.]]
[[Category: Phillips Jr GN]]
[[Category: McCoy, J G.]]
[[Category: Wesenberg GE]]
[[Category: Wesenberg, G E.]]
[[Category: candidate gene important in the pathogenesis of t-cell prolymphocytic leukemia]]
[[Category: center for eukaryotic structural genomic]]
[[Category: cesg]]
[[Category: gene associated with cre-pathway activation]]
[[Category: medically relevant]]
[[Category: protein structure initiative]]
[[Category: psi-2]]
[[Category: putative involvement in human inherited ataxias and disorders of purkinje cell degeneration]]
[[Category: structural genomic]]
[[Category: unknown function]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:31:15 2008''

Latest revision as of 08:43, 17 October 2024

Crystal structure of the uncharacterized human protein C8orf32 with bound peptideCrystal structure of the uncharacterized human protein C8orf32 with bound peptide

Structural highlights

3c9q is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

NTAQ1_HUMAN Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine (By similarity).

Evolutionary Conservation

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

3c9q, resolution 1.50Å

Drag the structure with the mouse to rotate

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