This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1py0

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Crystal structure of E51C/E54C Psaz from A.faecalis with CLaNP probe

Structural highlights

1py0 is a 1 chain structure with sequence from Alcaligenes faecalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AZUP_ALCFA This soluble electron transfer copper protein is required for the inactivation of copper-containing nitrite reductase in the presence of oxygen. Serves as a direct electron donor to the nitrite reductase.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

A lanthanide complex, named CLaNP (caged lanthanide NMR probe) has been developed for the characterisation of proteins by paramagnetic NMR spectroscopy. The probe consists of a lanthanide chelated by a derivative of DTPA (diethylenetriaminepentaacetic acid) with two thiol reactive functional groups. The CLaNP molecule is attached to a protein by two engineered, surface-exposed, Cys residues in a bidentate manner. This drastically limits the dynamics of the metal relative to the protein and enables measurements of pseudocontact shifts. NMR spectroscopy experiments on a diamagnetic control and the crystal structure of the probe-protein complex demonstrate that the protein structure is not affected by probe attachment. The probe is able to induce pseudocontact shifts to at least 40 A from the metal and causes residual dipolar couplings due to alignment at a high magnetic field. The molecule exists in several isomeric forms with different paramagnetic tensors; this provides a fast way to obtain long-range distance restraints.

A caged lanthanide complex as a paramagnetic shift agent for protein NMR.,Prudencio M, Rohovec J, Peters JA, Tocheva E, Boulanger MJ, Murphy ME, Hupkes HJ, Kosters W, Impagliazzo A, Ubbink M Chemistry. 2004 Jul 5;10(13):3252-60. PMID:15224334^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Prudencio M, Rohovec J, Peters JA, Tocheva E, Boulanger MJ, Murphy ME, Hupkes HJ, Kosters W, Impagliazzo A, Ubbink M. A caged lanthanide complex as a paramagnetic shift agent for protein NMR. Chemistry. 2004 Jul 5;10(13):3252-60. PMID:15224334 doi:10.1002/chem.200306019

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1py0"

@@ Line 3: / Line 3: @@
 <StructureSection load='1py0' size='340' side='right'caption='[[1py0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1py0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Alcfa Alcfa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PY0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PY0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1py0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PY0 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=Y1:YTTRIUM+ION'>Y1</scene>, <scene name='pdbligand=YMA:7,10,13-TRI(CARBOXYMETHYL)-5,15-DIOXO-4,7,10,13,16-PENTAAZA-1,19-DITHIANONADECANE'>YMA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</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&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1py0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1py0 OCA], [http://pdbe.org/1py0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1py0 RCSB], [http://www.ebi.ac.uk/pdbsum/1py0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1py0 ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=Y1:YTTRIUM+ION'>Y1</scene>, <scene name='pdbligand=YMA:7,10,13-TRI(CARBOXYMETHYL)-5,15-DIOXO-4,7,10,13,16-PENTAAZA-1,19-DITHIANONADECANE'>YMA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1py0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1py0 OCA], [https://pdbe.org/1py0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1py0 RCSB], [https://www.ebi.ac.uk/pdbsum/1py0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1py0 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/AZUP_ALCFA AZUP_ALCFA]] This soluble electron transfer copper protein is required for the inactivation of copper-containing nitrite reductase in the presence of oxygen. Serves as a direct electron donor to the nitrite reductase.
+[https://www.uniprot.org/uniprot/AZUP_ALCFA AZUP_ALCFA] This soluble electron transfer copper protein is required for the inactivation of copper-containing nitrite reductase in the presence of oxygen. Serves as a direct electron donor to the nitrite reductase.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Alcfa]]
+[[Category: Alcaligenes faecalis]]
 [[Category: Large Structures]]
-[[Category: Boulanger, M J]]
+[[Category: Boulanger MJ]]
-[[Category: Hupkes, H J]]
+[[Category: Hupkes HJ]]
-[[Category: Impagliazzo, A]]
+[[Category: Impagliazzo A]]
-[[Category: Kosters, W]]
+[[Category: Kosters W]]
-[[Category: Murphy, M E]]
+[[Category: Murphy ME]]
-[[Category: Peters, J A]]
+[[Category: Peters JA]]
-[[Category: Prudencio, M]]
+[[Category: Prudencio M]]
-[[Category: Rohovec, J]]
+[[Category: Rohovec J]]
-[[Category: Tocheva, E]]
+[[Category: Tocheva E]]
-[[Category: Ubbink, M]]
+[[Category: Ubbink M]]
-[[Category: Cupredoxin]]
-[[Category: Electron transport]]
-[[Category: Nmr probe]]

1py0

From Proteopedia

Current revision

Crystal structure of E51C/E54C Psaz from A.faecalis with CLaNP probe

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox