2b3k: Difference between revisions
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[[Image:2b3k.gif|left|200px]] | [[Image:2b3k.gif|left|200px]] | ||
'''Crystal structure of Human Methionine Aminopeptidase Type I in the holo form''' | {{Structure | ||
|PDB= 2b3k |SIZE=350|CAPTION= <scene name='initialview01'>2b3k</scene>, resolution 1.550Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] | |||
|GENE= METAP1, KIAA0094 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Crystal structure of Human Methionine Aminopeptidase Type I in the holo form''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2B3K is a [ | 2B3K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B3K OCA]. | ||
==Reference== | ==Reference== | ||
Structural basis for the functional differences between type I and type II human methionine aminopeptidases., Addlagatta A, Hu X, Liu JO, Matthews BW, Biochemistry. 2005 Nov 15;44(45):14741-9. PMID:[http:// | Structural basis for the functional differences between type I and type II human methionine aminopeptidases., Addlagatta A, Hu X, Liu JO, Matthews BW, Biochemistry. 2005 Nov 15;44(45):14741-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16274222 16274222] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Methionyl aminopeptidase]] | [[Category: Methionyl aminopeptidase]] | ||
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[[Category: petabread fold]] | [[Category: petabread fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:57:06 2008'' | ||
Revision as of 16:57, 20 March 2008
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| , resolution 1.550Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Gene: | METAP1, KIAA0094 (Homo sapiens) | ||||||
| Activity: | Methionyl aminopeptidase, with EC number 3.4.11.18 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Human Methionine Aminopeptidase Type I in the holo form
OverviewOverview
Determination of the crystal structure of human MetAP1 makes it possible, for the first time, to compare the structures of a Type I and a Type II methionine aminopeptidase (MetAP) from the same organism. Comparison of the Type I enzyme with the previously reported complex of ovalicin with Type II MetAP shows that the active site of the former is reduced in size and would incur steric clashes with the bound inhibitor. This explains why ovalicin and related anti-angiogenesis inhibitors target Type II human MetAP but not Type I. The differences in both size and shape of the active sites between MetAP1 and MetAP2 also help to explain their different substrate specificity. In the presence of excess Co(2+), a third cobalt ion binds in the active site region, explaining why metal ions in excess can be inhibitory. Also, the N-terminal region of the protein contains three distinct Pro-x-x-Pro motifs, supporting the prior suggestion that this region of the protein may participate in binding to the ribosome.
About this StructureAbout this Structure
2B3K is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for the functional differences between type I and type II human methionine aminopeptidases., Addlagatta A, Hu X, Liu JO, Matthews BW, Biochemistry. 2005 Nov 15;44(45):14741-9. PMID:16274222
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