GMP synthase: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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 <StructureSection load='2vxo' size='400' side='right' caption='Structure of human GMP synthase dimer complex with xantosine 5-phosphate and sulfate  (PDB entry [[2vxo]])' scene='51/516475/Cv/1'>
 == Function ==
-'''GMP synthase''' (GMPS) catalyzes the conversion of xantosine 5’-phosphate (XMP), ATP, glutamine and water to glutamate, GMP, AMP and diphosphate.  GMPS is active in purine and glutamate metabolism<ref>PMID:24462112</ref>.  GMPS is a bifunctional two-domain enzyme with the <scene name='51/516475/Cv/2'>N-terminal glutaminase</scene> dominates extracts ammonia from glutamine and the <scene name='51/516475/Cv/3'>C-terminal synthetase</scene> adds amine group to XMP to produce GMP.
+'''GMP synthase''' (GMPS) catalyzes the conversion of xantosine 5’-phosphate (XMP), ATP, glutamine and water to glutamate, GMP, AMP and diphosphate.  GMPS is active in purine and glutamate metabolism<ref>PMID:24462112</ref>.  GMPS is a bifunctional two-domain enzyme with the <scene name='51/516475/Cv/12'>N-terminal glutaminase</scene> dominates extracts ammonia from glutamine and the <scene name='51/516475/Cv/13'>C-terminal synthetase</scene> adds amine group to XMP to produce GMP.
 == Structural highlights ==
-Human GMPS structure contains <scene name='51/516475/Cv/10'>2 dimerization domains (D1 and D2)</scene>.  The <scene name='51/516475/Cv/6'>active site is located between the synthetase domain and D2 domain and covered by the LID motif</scene>.  <scene name='51/516475/Cv/9'>Whole active site</scene><ref>PMID:23816837</ref>.
+Human GMPS structure contains <scene name='51/516475/Cv/14'>2 dimerization domains (D1 and D2)</scene>.  The <scene name='51/516475/Cv/15'>active site is located between the synthetase domain and D2 domain and covered by the LID motif</scene>.  <scene name='51/516475/Cv/16'>Whole active site</scene>. N-terminal glutaminase domain contains <scene name='51/516475/Cv/17'>catalytic triad Cys104, His190, Glu192</scene><ref>PMID:23816837</ref>.
 ==3D structures of GMP synthase==
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 Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+[[2vpi]] – hGMPS glutaminase domain – human<br />
+[[2vxo]] - hGMPS + XMP<br />
 [[1wl8]], [[2d7j]] – PhGMPS subunit A – ''Pyrococcus horikoshii''<br />
 [[2dpl]], [[3a4i]] - PhGMPS subunit B<br />
 [[2ywb]] – TtGMPS – ''Thermus thermophilus''<br />
+[[2ywc]] – TtGMPS + XMP<br />
 [[3tqi]] – GMPS – ''Coxiella burnetii''<br />
 [[1kxj]] – TmGMPS – ''Thermotoga maritima''<br />
+[[2iss]] – TmGMPS subunit PDXT + PLP biosynthesis lyase PDXS<br />
 [[2a9v]] – GMPS – ''Thermoplasma acidophilum''<br />
-[[2lxn]] – GMPS subunit A – ''Methanocaldococcus jannaschii''<br />
+[[2lxn]], [[7d40]], [[7d95]] – MjGMPS subunit A – ''Methanocaldococcus jannaschii''<br />
-[[2vpi]] – hGMPS glutaminase domain – human<br />
+[[7d96]], [[7d97]] – MjGMPS subunit A (mutant)<br />
-[[2vxo]] - hGMPS + XMP<br />
+[[6jp9]] – MjGMPS subunit B + XMP<br />
-[[2ywc]] – TtGMPS + XMP<br />
+[[1gpm]] – GMPS + pyrophosphate + AMP – ''Escherichia coli''<br />
-[[2iss]] – TmGMPS subunit PDXT + PLP biosynthesis lyase PDXS<br />
+[[5tw7]] – GMPS – ''Neisseria gonorrhoeae''<br />
-[[1gpm]] – GMPS + pyrophosphate + AMP – ''Escherichia coli''
+[[7mo6]] – GMPS – ''Aspergillus fumigatus''<br />
+[[7sbc]] – GMPS – ''Acinetobacter baumannii''<br />
 == References ==
 <references/>
 </StructureSection>
 [[Category:Topic Page]]