PROSITE documentation PDOC51855 [for PROSITE entry PS51855]

MGS-like domain profile





Description

Methylglyoxal synthase (MGS, EC 4.2.3.3) (see <PDOC01037>), which catalyzes the conversion of dihydroxyacetone phosphate (DHAP) to methylglyoxal (MG) and inorganic phosphate, has been found in many organisms, including enteric bacteria, some gram-positive bacteria, a number of archaebacteria, several yeast species and goat liver [1,2]. A domain similar to the full-length MGS is found in [3]:

  • Bifunctional purine biosynthesis protein PurH, also known as aminoimidazole-4-carboxamide ribonucleotide (AICAR) transformylase (AICAR Tfase)/inosine 50-monophosphate (IMP) cyclohydrolase (IMPCH) (ATIC) (EC 2.1.2.3). In bacteria and eukaryotes, the last two steps of de novo purine biosynthesis are catalyzed by PurH, which is composed of two functionally independent domains linked by a flexible region. The N- terminal MGS-like domain possesses IMPCH activity and the C-terminal domain possesses AICAR Tfase activity. The MGS-like domain with IMPCH activity catalyzes the intramolecular cyclization of 5-formyl-AICAR (FAICAR) to IMP [4,5,6,7].
  • Carbamoyl phosphate synthetase (CPS) catalyzes the formation of carbamoyl phosphate from one molecule of bicarbonate, two molecules of Mg(2+)ATP and one molecule of glutamine or ammonia depending upon the particular form of the enzyme. The enzyme is an α,β-heterodimer consisting of a small subunit that hydrolyzes glutamine and a large subunit that catalyzes the two required phosphorylation events. The large subunit consists of four structural units: the carboxyphosphate synthetic component, the oligomerization domain, the carbamoyl phosphate synthetic component and the MGS-like allosteric domain. The binding of various ligands by the MGS-like domain allosterically regulates CPS [8,9].

The main core of the MGS-like domain, a modified 'Rossmann' fold, is characterized by a five stranded parallel β-sheet flanked on either side by three and five α-helices, respectively (see <PDB:1PKX>) [6,8]. MGS-like domains share a conserved phosphate binding site [3,7].

The profile we developed covers the entire MGS-like domain.

Last update:

January 2018 / First entry.

Technical section

PROSITE method (with tools and information) covered by this documentation:

MGS, PS51855; MGS-like domain profile  (MATRIX)


References

1AuthorsFalahati H., Pazhang M., Zareian S., Ghaemi N., Rofougaran R., Hofer A., Rezaie A.R., Khajeh K.
TitleTransmitting the allosteric signal in methylglyoxal synthase.
SourceProtein Eng. Des. Sel. 26:445-452(2013).
PubMed ID23592737
DOI10.1093/protein/gzt014

2AuthorsHuang K., Rudolph F.B., Bennett G.N.
TitleCharacterization of methylglyoxal synthase from Clostridium acetobutylicum ATCC 824 and its use in the formation of 1, 2-propanediol.
SourceAppl. Environ. Microbiol. 65:3244-3247(1999).
PubMed ID10388730

3AuthorsMurzin A.G.
TitleStructure classification-based assessment of CASP3 predictions for the fold recognition targets.
SourceProteins 0:88-103(1999).
PubMed ID10526357

4AuthorsQiu X., Yuan Y., Gao Y.
TitleExpression, purification, crystallization and preliminary X-ray diffraction crystallographic study of PurH from Escherichia coli.
SourceActa Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 67:1590-1594(2011).
PubMed ID22139174
DOI10.1107/S1744309111039960

5AuthorsAxelrod H.L., McMullan D., Krishna S.S., Miller M.D., Elsliger M.-A., Abdubek P., Ambing E., Astakhova T., Carlton D., Chiu H.-J., Clayton T., Duan L., Feuerhelm J., Grzechnik S.K., Hale J., Han G.W., Haugen J., Jaroszewski L., Jin K.K., Klock H.E., Knuth M.W., Koesema E., Morse A.T., Nigoghossian E., Okach L., Oommachen S., Paulsen J., Quijano K., Reyes R., Rife C.L., van den Bedem H., Weekes D., White A., Wolf G., Xu Q., Hodgson K.O., Wooley J., Deacon A.M., Godzik A., Lesley S.A., Wilson I.A.
TitleCrystal structure of AICAR transformylase IMP cyclohydrolase (TM1249) from Thermotoga maritima at 1.88 A resolution.
SourceProteins 71:1042-1049(2008).
PubMed ID18260100
DOI10.1002/prot.21967

6AuthorsWolan D.W., Cheong C.-G., Greasley S.E., Wilson I.A.
TitleStructural insights into the human and avian IMP cyclohydrolase mechanism via crystal structures with the bound XMP inhibitor.
SourceBiochemistry 43:1171-1183(2004).
PubMed ID14756553
DOI10.1021/bi030162i

7AuthorsVerma P., Kar B., Varshney R., Roy P., Sharma A.K.
TitleCharacterization of AICAR transformylase/IMP cyclohydrolase (ATIC) from Staphylococcus lugdunensis.
SourceFEBS J. 284:4233-4261(2017).
PubMed ID29063699
DOI10.1111/febs.14303

8AuthorsThoden J.B., Raushel F.M., Benning M.M., Rayment I., Holden H.M.
TitleThe structure of carbamoyl phosphate synthetase determined to 2.1 A resolution.
SourceActa Crystallogr. D 55:8-24(1999).
PubMed ID10089390
DOI10.1107/S0907444998006234

9Authorsde Cima S., Polo L.M., Diez-Fernandez C., Martinez A.I., Cervera J., Fita I., Rubio V.
TitleStructure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis.
SourceSci. Rep. 5:16950-16950(2015).
PubMed ID26592762
DOI10.1038/srep16950



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