5u03: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

The entry ~~5u03~~ is ~~ON HOLD~~

==Cryo-EM structure of the human CTP synthase filament==

~~Authors~~:

== Structural highlights ==

<table><tr><td colspan='2'>[[5u03]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U03 OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5U03 FirstGlance].

~~Description~~:

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</scene></td></tr>

[[Category: ~~Unreleased Structures~~]]

<tr id='related'><td class="sblockLbl">[[Related_structure|Related:]]</td><td class="sblockDat">[[5u05|5u05]]</td></tr>

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[http://en.wikipedia.org/wiki/CTP_synthase_(glutamine_hydrolyzing) CTP synthase (glutamine hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.2 6.3.4.2] </td></tr>

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5u03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u03 OCA], [http://pdbe.org/5u03 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u03 RCSB], [http://www.ebi.ac.uk/pdbsum/5u03 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u03 ProSAT]</td></tr>

</table>

== Disease ==

[[http://www.uniprot.org/uniprot/PYRG1_HUMAN PYRG1_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry. A unique and recessive G to C mutation probably affecting a splice donor site at the junction of intron 17-18 and exon 18 has been identified in all patients. It results in expression of an abnormal transcript lacking exon 18 and a complete loss of the expression of the protein.<ref>PMID:24870241</ref>

== Function ==

[[http://www.uniprot.org/uniprot/PYRG1_HUMAN PYRG1_HUMAN]] This enzyme is involved in the de novo synthesis of CTP, a precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as a source of nitrogen. This enzyme and its product, CTP, play a crucial role in the proliferation of activated lymphocytes and therefore in immunity.<ref>PMID:16179339</ref> <ref>PMID:24870241</ref>

== References ==

__TOC__

</StructureSection>

[[Category: Kollman, J M]]

[[Category: Lynch, E M]]

[[Category: Enzyme]]

[[Category: Filament]]

[[Category: Ligase]]

[[Category: Nucleotide metabolism]]

[[Category: Protein fibril]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5u03 is ON HOLD
+==Cryo-EM structure of the human CTP synthase filament==
+<StructureSection load='5u03' size='340' side='right' caption='[[5u03]], [[Resolution|resolution]] 6.10&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5u03]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U03 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5U03 FirstGlance]. <br>
-Description:
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5u05|5u05]]</td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/CTP_synthase_(glutamine_hydrolyzing) CTP synthase (glutamine hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.2 6.3.4.2] </span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5u03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u03 OCA], [http://pdbe.org/5u03 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u03 RCSB], [http://www.ebi.ac.uk/pdbsum/5u03 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u03 ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[[http://www.uniprot.org/uniprot/PYRG1_HUMAN PYRG1_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry. A unique and recessive G to C mutation probably affecting a splice donor site at the junction of intron 17-18 and exon 18 has been identified in all patients. It results in expression of an abnormal transcript lacking exon 18 and a complete loss of the expression of the protein.<ref>PMID:24870241</ref>
+== Function ==
+[[http://www.uniprot.org/uniprot/PYRG1_HUMAN PYRG1_HUMAN]] This enzyme is involved in the de novo synthesis of CTP, a precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as a source of nitrogen. This enzyme and its product, CTP, play a crucial role in the proliferation of activated lymphocytes and therefore in immunity.<ref>PMID:16179339</ref> <ref>PMID:24870241</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Kollman, J M]]
+[[Category: Lynch, E M]]
+[[Category: Enzyme]]
+[[Category: Filament]]
+[[Category: Ligase]]
+[[Category: Nucleotide metabolism]]
+[[Category: Protein fibril]]