PROSITE documentation PDOC52013Zinc finger C6H2-type profile
Methionine Aminopeptidases (MetAPs) are "metalloenzymes" primarily responsible for the co-translational cleavage of the initial methionine residue from the nascent polypeptides. MetAPs are classified into two isoforms: namely, MetAP1 and MetAP2. Only one type of MetAP, either type 1 or type 2, can be found in a prokaryotic cell. Archaea contain type 2 MetAPs, and eubacteria contain type 1 MetAPs. However, all eukaryotic genomes studied to date encode at least a cytosolic type 1 MetAP and a cytosolic type 2 MetAP. All MetAPs C-terminal catalytic domains are conserved in both prokaryotes and eukaryotes. Extensions at the N-terminus of the catalytic domain of eukaryotic cytosolic MetAPs distinguish them from their prokaryotic counterparts. Within this N-terminal region, MetAP1 has a C6H2-type zinc finger, with four pairs of conserved cysteine and histidine residues and conserved aromatic residues. The C6H2-type zinc finger is essential for the normal processing function of MetAP1 and may be important for the proper functional alignment of MetAP1 on the ribosomes. It is a protein-protein interaction domain [1,2,3,4].
The structure of the C6H2-type zinc finger shows a ββαβα cross-brace fold with a 1,3,2 antiparallel β-sheet (see <PDB:7SEK>). Zn1 is coordinated by C1, C2, C5, and C6, and Zn2 by C3, C4, H7, and H8 [4].
The profile we developed covers the entire C6H2-type zinc finger.
Last update:December 2022 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Weako J. Uba A.I. Keskin O. Guersoy A. Yelekci K. |
| Title | Identification of potential inhibitors of human methionine aminopeptidase (type II) for cancer therapy: Structure-based virtual screening, ADMET prediction and molecular dynamics studies. | |
| Source | Comput. Biol. Chem. 86:107244-107244(2020). | |
| PubMed ID | 32252002 | |
| DOI | 10.1016/j.compbiolchem.2020.107244 |
| 2 | Authors | Zhang F. Bhat S. Gabelli S.B. Chen X. Miller M.S. Nacev B.A. Cheng Y.L. Meyers D.J. Tenney K. Shim J.S. Crews P. Amzel L.M. Ma D. Liu J.O. |
| Title | Pyridinylquinazolines selectively inhibit human methionine aminopeptidase-1 in cells. | |
| Source | J. Med. Chem. 56:3996-4016(2013). | |
| PubMed ID | 23634668 | |
| DOI | 10.1021/jm400227z |
| 3 | Authors | Vetro J.A. Chang Y.-H. |
| Title | Yeast methionine aminopeptidase type 1 is ribosome-associated and requires its N-terminal zinc finger domain for normal function in vivo. | |
| Source | J. Cell. Biochem. 85:678-688(2002). | |
| PubMed ID | 11968008 | |
| DOI | 10.1002/jcb.10161 |
| 4 | Authors | Weiss A. Murdoch C.C. Edmonds K.A. Jordan M.R. Monteith A.J. Perera Y.R. Rodriguez Nassif A.M. Petoletti A.M. Beavers W.N. Munneke M.J. Drury S.L. Krystofiak E.S. Thalluri K. Wu H. Kruse A.R.S. DiMarchi R.D. Caprioli R.M. Spraggins J.M. Chazin W.J. Giedroc D.P. Skaar E.P. |
| Title | Zn-regulated GTPase metalloprotein activator 1 modulates vertebrate zinc homeostasis. | |
| Source | Cell 185:2148-2163.e27(2022). | |
| PubMed ID | 35584702 | |
| DOI | 10.1016/j.cell.2022.04.011 |
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