1a16

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:26, 7 February 2024) (edit) (undo)
 
(13 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1a16.gif|left|200px]]
 
-
<!--
+
==AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU==
-
The line below this paragraph, containing "STRUCTURE_1a16", creates the "Structure Box" on the page.
+
<StructureSection load='1a16' size='340' side='right'caption='[[1a16]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1a16]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A16 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
-
{{STRUCTURE_1a16| PDB=1a16 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a16 OCA], [https://pdbe.org/1a16 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a16 RCSB], [https://www.ebi.ac.uk/pdbsum/1a16 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a16 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/AMPP_ECOLI AMPP_ECOLI]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a1/1a16_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a16 ConSurf].
 +
<div style="clear:both"></div>
-
'''AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU'''
+
==See Also==
-
 
+
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
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 Structure==
+
-
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==
+
-
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: Large Structures]]
-
[[Category: Xaa-Pro aminopeptidase]]
+
[[Category: Bond CS]]
-
[[Category: Bond, C S.]]
+
[[Category: Dixon NE]]
-
[[Category: Dixon, N E.]]
+
[[Category: Freeman HC]]
-
[[Category: Freeman, H C.]]
+
[[Category: Guss JM]]
-
[[Category: Guss, J M.]]
+
[[Category: Lilley PE]]
-
[[Category: Lilley, P E.]]
+
[[Category: Wilce MC]]
-
[[Category: Wilce, M C.]]
+
-
[[Category: Proline peptidase]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:50:36 2008''
+

Current revision

AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU

PDB ID 1a16

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1a16"
Personal tools