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.

4awn

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 05:48, 25 August 2022

Structure of recombinant human DNase I (rhDNaseI) in complex with Magnesium and Phosphate.

Structural highlights

4awn is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Activity:	Deoxyribonuclease I, with EC number 3.1.21.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[DNAS1_HUMAN] Systemic lupus erythematosus. Disease susceptibility is associated with variations affecting the gene represented in this entry.

Function

[DNAS1_HUMAN] Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization (By similarity).

Publication Abstract from PubMed

Recombinant human DNase I (Pulmozyme, dornase alfa) is used for the treatment of cystic fibrosis where it improves lung function and reduces the number of exacerbations. The physiological mechanism of action is thought to involve the reduction of the viscoelasticity of cystic fibrosis sputum by hydrolyzing high concentrations of DNA into low-molecular mass fragments. Here we describe the 1.95 A resolution crystal structure of recombinant human DNase I (rhDNase I) in complex with magnesium and phosphate ions, both bound in the active site. Complementary mutagenesis data of rhDNase I coupled to a comprehensive structural analysis of the DNase I-like superfamily argue for the key catalytic role of Asn7, which is invariant among mammalian DNase I enzymes and members of this superfamily, through stabilization of the magnesium ion coordination sphere. Overall, our combined structural and mutagenesis data suggest the occurrence of a magnesium-assisted pentavalent phosphate transition state in human DNase I during catalysis, where Asp168 may play a key role as a general catalytic base.

The Structure of Human DNase I Bound to Magnesium and Phosphate Ions Points to a Catalytic Mechanism Common to Members of the DNase I-like Superfamily.,Parsiegla G, Noguere C, Santell L, Lazarus RA, Bourne Y Biochemistry. 2012 Dec 21;51(51):10250-8. doi: 10.1021/bi300873f. Epub 2012 Dec, 13. PMID:23215638^[1]

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

References

↑ Parsiegla G, Noguere C, Santell L, Lazarus RA, Bourne Y. The Structure of Human DNase I Bound to Magnesium and Phosphate Ions Points to a Catalytic Mechanism Common to Members of the DNase I-like Superfamily. Biochemistry. 2012 Dec 21;51(51):10250-8. doi: 10.1021/bi300873f. Epub 2012 Dec, 13. PMID:23215638 doi:http://dx.doi.org/10.1021/bi300873f

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4awn"

@@ Line 3: / Line 3: @@
 <StructureSection load='4awn' size='340' side='right'caption='[[4awn]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4awn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AWN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AWN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4awn]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AWN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AWN FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Deoxyribonuclease_I Deoxyribonuclease I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.1 3.1.21.1] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Deoxyribonuclease_I Deoxyribonuclease I], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.1 3.1.21.1] </span></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=4awn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4awn OCA], [http://pdbe.org/4awn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4awn RCSB], [http://www.ebi.ac.uk/pdbsum/4awn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4awn ProSAT]</span></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=4awn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4awn OCA], [https://pdbe.org/4awn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4awn RCSB], [https://www.ebi.ac.uk/pdbsum/4awn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4awn ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/DNAS1_HUMAN DNAS1_HUMAN]] Systemic lupus erythematosus. Disease susceptibility is associated with variations affecting the gene represented in this entry.
+[[https://www.uniprot.org/uniprot/DNAS1_HUMAN DNAS1_HUMAN]] Systemic lupus erythematosus. Disease susceptibility is associated with variations affecting the gene represented in this entry.
 == Function ==
-[[http://www.uniprot.org/uniprot/DNAS1_HUMAN DNAS1_HUMAN]] Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization (By similarity).
+[[https://www.uniprot.org/uniprot/DNAS1_HUMAN DNAS1_HUMAN]] Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 26: / Line 26: @@
 </StructureSection>
 [[Category: Deoxyribonuclease I]]
-[[Category: Human]]
 [[Category: Large Structures]]
 [[Category: Bourne, Y]]

4awn

From Proteopedia

Revision as of 05:48, 25 August 2022

Structure of recombinant human DNase I (rhDNaseI) in complex with Magnesium and Phosphate.

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox