1a16: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1a16 |SIZE=350|CAPTION= <scene name='initialview01'>1a16</scene>, resolution 2.3Å | |PDB= 1a16 |SIZE=350|CAPTION= <scene name='initialview01'>1a16</scene>, resolution 2.3Å | ||
|SITE= <scene name='pdbsite=NUL:These+Residues+Coordinate+The+Mn+Ions'>NUL</scene> | |SITE= <scene name='pdbsite=NUL:These+Residues+Coordinate+The+Mn+Ions'>NUL</scene> | ||
|LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a16 OCA], [http://www.ebi.ac.uk/pdbsum/1a16 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a16 RCSB]</span> | |||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Lilley, P E.]] | [[Category: Lilley, P E.]] | ||
[[Category: Wilce, M C.]] | [[Category: Wilce, M C.]] | ||
[[Category: complex (proline peptidase/inhibitor)]] | [[Category: complex (proline peptidase/inhibitor)]] | ||
[[Category: proline peptidase]] | [[Category: proline peptidase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:30:54 2008'' | ||
Revision as of 18:30, 30 March 2008
| |||||||
| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Xaa-Pro aminopeptidase, with EC number 3.4.11.9 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU
OverviewOverview
The structure of the proline-specific aminopeptidase (EC 3.4.11.9) from Escherichia coli has been solved and refined for crystals of the native enzyme at a 2.0-A resolution, for a dipeptide-inhibited complex at 2.3-A resolution, and for a low-pH inactive form at 2.7-A resolution. The protein crystallizes as a tetramer, more correctly a dimer of dimers, at both high and low pH, consistent with observations from analytical ultracentrifuge studies that show that the protein is a tetramer under physiological conditions. The monomer folds into two domains. The active site, in the larger C-terminal domain, contains a dinuclear manganese center in which a bridging water molecule or hydroxide ion appears poised to act as the nucleophile in the attack on the scissile peptide bond of Xaa-Pro. The metal-binding residues are located in a single subunit, but the residues surrounding the active site are contributed by three subunits. The fold of the protein resembles that of creatine amidinohydrolase (creatinase, not a metalloenzyme). The C-terminal catalytic domain is also similar to the single-domain enzyme methionine aminopeptidase that has a dinuclear cobalt center.
About this StructureAbout this Structure
1A16 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli., Wilce MC, Bond CS, Dixon NE, Freeman HC, Guss JM, Lilley PE, Wilce JA, Proc Natl Acad Sci U S A. 1998 Mar 31;95(7):3472-7. PMID:9520390
Page seeded by OCA on Sun Mar 30 18:30:54 2008