1a16: Difference between revisions
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[[Image:1a16.gif|left|200px]] | [[Image:1a16.gif|left|200px]] | ||
'''AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU''' | {{Structure | ||
|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> | |||
|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] | |||
|GENE= | |||
}} | |||
'''AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1A16 is a [ | 1A16 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A16 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9520390 9520390] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: proline peptidase]] | [[Category: proline peptidase]] | ||
''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 09:51:22 2008'' | ||
Revision as of 10:51, 20 March 2008
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| , resolution 2.3Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Xaa-Pro aminopeptidase, with EC number 3.4.11.9 | ||||||
| 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
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