GMP synthase: Difference between revisions

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<StructureSection load='2vxo' size='400' side='right' caption='Structure of human GMP synthase complex with xantosine 5-phosphate  (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 ==
'''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.


'''GMP synthase''' (GMPS) catalyzes the conversion of xantosine 5’-phosphate, ATP, glutamine and water to glutamate, GMP, AMP and diphosphate.  GMPS is active in purine and glutamate metabolism.
== Structural highlights ==
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==
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 />
[[2yw7]] – 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 />
[[2vpi]] – hGMPS glutaminase domain – human<br />
[[2vxo]] - hGMPS + xantosine 5’-phosphate<br />
[[2ywc]] – TtGMPS + xantosine 5’-phosphate<br />
[[2iss]] – TmGMPS subunit PDXT + PLP biosynthesis lyase PDXS<br />
[[2iss]] – TmGMPS subunit PDXT + PLP biosynthesis lyase PDXS<br />
[[1gpm]] – GMPS + pyrophosphate + AMP – ''Escherichia coli''
[[2a9v]] – GMPS – ''Thermoplasma acidophilum''<br />
 
[[2lxn]], [[7d40]], [[7d95]] – MjGMPS subunit A – ''Methanocaldococcus jannaschii''<br />
[[7d96]], [[7d97]] – MjGMPS subunit A (mutant)<br />
[[6jp9]] – MjGMPS subunit B + XMP<br />
[[1gpm]] – GMPS + pyrophosphate + AMP – ''Escherichia coli''<br />
[[5tw7]] – GMPS – ''Neisseria gonorrhoeae''<br />
[[7mo6]] – GMPS – ''Aspergillus fumigatus''<br />
[[7sbc]] – GMPS – ''Acinetobacter baumannii''<br />
== References ==
<references/>
</StructureSection>
</StructureSection>
[[Category:Topic Page]]

Latest revision as of 10:58, 10 April 2023

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[1]. GMPS is a bifunctional two-domain enzyme with the dominates extracts ammonia from glutamine and the adds amine group to XMP to produce GMP.

Structural highlights

Human GMPS structure contains . The . . N-terminal glutaminase domain contains [2].

3D structures of GMP synthase

Updated on 04-May-2025

2vpi – hGMPS glutaminase domain – human

2vxo - hGMPS + XMP
1wl8, 2d7j – PhGMPS subunit A – Pyrococcus horikoshii
2dpl, 3a4i - PhGMPS subunit B
2ywb – TtGMPS – Thermus thermophilus
2ywc – TtGMPS + XMP
3tqi – GMPS – Coxiella burnetii
1kxj – TmGMPS – Thermotoga maritima
2iss – TmGMPS subunit PDXT + PLP biosynthesis lyase PDXS
2a9v – GMPS – Thermoplasma acidophilum
2lxn, 7d40, 7d95 – MjGMPS subunit A – Methanocaldococcus jannaschii
7d96, 7d97 – MjGMPS subunit A (mutant)
6jp9 – MjGMPS subunit B + XMP
1gpm – GMPS + pyrophosphate + AMP – Escherichia coli
5tw7 – GMPS – Neisseria gonorrhoeae
7mo6 – GMPS – Aspergillus fumigatus
7sbc – GMPS – Acinetobacter baumannii

References

  1. ↑ Reddy BA, van der Knaap JA, Bot AG, Mohd-Sarip A, Dekkers DH, Timmermans MA, Martens JW, Demmers JA, Verrijzer CP. Nucleotide biosynthetic enzyme GMP synthase is a TRIM21-controlled relay of p53 stabilization. Mol Cell. 2014 Feb 6;53(3):458-70. doi: 10.1016/j.molcel.2013.12.017. Epub 2014, Jan 23. PMID:24462112 doi:http://dx.doi.org/10.1016/j.molcel.2013.12.017
  2. ↑ Welin M, Lehtio L, Johansson A, Flodin S, Nyman T, Tresaugues L, Hammarstrom M, Graslund S, Nordlund P. Substrate Specificity and Oligomerization of Human GMP Synthetase. J Mol Biol. 2013 Jun 28. pii: S0022-2836(13)00427-0. doi:, 10.1016/j.jmb.2013.06.032. PMID:23816837 doi:10.1016/j.jmb.2013.06.032

Structure of human GMP synthase dimer complex with xantosine 5-phosphate and sulfate (PDB entry 2vxo)

Drag the structure with the mouse to rotate

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Michal Harel, Alexander Berchansky
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