GMP synthase: Difference between revisions

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<StructureSection load='2vxo' size='400' side='right' caption='Structure of human GMP synthase dimer complex with xantosine 5-phosphate (stick model) and sulfate  (PDB entry [[2vxo]])' scene=''>
<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 ==
== 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 N-terminal glutaminase dominates extracts ammonia from glutamine and the C-terminal synthetase 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 ==
== Structural highlights ==
Human GMPS structure contains 2 dimerization domains (D1 and D2).  The active site is located between the synthetase domain and D2 domain and covered by the LID motif.  The catalytic triad consists of Cys, His and Glu<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==
==3D structures of GMP synthase==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
   
   
[[2vpi]] – hGMPS glutaminase domain – human<br />
[[2vxo]] - hGMPS + XMP<br />
[[1wl8]], [[2d7j]] – PhGMPS subunit A – ''Pyrococcus horikoshii''<br />
[[1wl8]], [[2d7j]] – PhGMPS subunit A – ''Pyrococcus horikoshii''<br />
[[2dpl]], [[3a4i]] - PhGMPS subunit B<br />
[[2dpl]], [[3a4i]] - PhGMPS subunit B<br />
[[2ywb]] – TtGMPS – ''Thermus thermophilus''<br />
[[2ywb]] – TtGMPS – ''Thermus thermophilus''<br />
[[2ywc]] – TtGMPS + XMP<br />
[[3tqi]] – GMPS – ''Coxiella burnetii''<br />
[[3tqi]] – GMPS – ''Coxiella burnetii''<br />
[[1kxj]] – TmGMPS – ''Thermotoga maritima''<br />
[[1kxj]] – TmGMPS – ''Thermotoga maritima''<br />
[[2iss]] – TmGMPS subunit PDXT + PLP biosynthesis lyase PDXS<br />
[[2a9v]] – GMPS – ''Thermoplasma acidophilum''<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 ==
<references/>
<references/>
</StructureSection>
</StructureSection>
[[Category:Topic Page]]
[[Category:Topic Page]]

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

Michal Harel, Alexander Berchansky