1jq6

From Proteopedia

(Difference between revisions)

Current revision

HUMAN CYTOMEGALOVIRUS PROTEASE DIMER-INTERFACE MUTANT, S225Y

Structural highlights

1jq6 is a 1 chain structure with sequence from Human betaherpesvirus 5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SCAF_HCMVA Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein UL86 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein UL86. Cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging (By similarity). Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein UL86. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging (By similarity).

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

Biochemical studies indicate that dimerization is required for the catalytic activity of herpesvirus proteases, whereas structural studies show a complete active site in each monomer, away from the dimer interface. Here we report kinetic, biophysical and crystallographic characterizations of structure-based mutants in the dimer interface of human cytomegalovirus (HCMV) protease. Such mutations can produce a 1,700-fold reduction in the kcat while having minimal effects on the K(m). Dimer stability is not affected by these mutations, suggesting that dimerization itself is insufficient for activity. There are large changes in monomer conformation and dimer organization of the apo S225Y mutant enzyme. However, binding of an activated peptidomimetic inhibitor induced a conformation remarkably similar to the wild type protease. Our studies suggest that appropriate dimer formation may be required to indirectly stabilize the protease oxyanion hole, revealing a novel mechanism for dimerization to regulate enzyme activity.

Molecular mechanism for dimerization to regulate the catalytic activity of human cytomegalovirus protease.,Batra R, Khayat R, Tong L Nat Struct Biol. 2001 Sep;8(9):810-7. PMID:11524687^[1]

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

References

↑ Batra R, Khayat R, Tong L. Molecular mechanism for dimerization to regulate the catalytic activity of human cytomegalovirus protease. Nat Struct Biol. 2001 Sep;8(9):810-7. PMID:11524687 doi:http://dx.doi.org/10.1038/nsb0901-810

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/1jq6"

Categories: Human betaherpesvirus 5 | Large Structures | Batra R | Khayat R | Tong L

@@ Line 1: / Line 1: @@
-[[Image:1jq6.jpg|left|200px]]<br /><applet load="1jq6" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1jq6, resolution 2.30&Aring;" />
-'''HUMAN CYTOMEGALOVIRUS PROTEASE DIMER-INTERFACE MUTANT, S225Y'''<br />
-==Overview==
+==HUMAN CYTOMEGALOVIRUS PROTEASE DIMER-INTERFACE MUTANT, S225Y==
-Biochemical studies indicate that dimerization is required for the, catalytic activity of herpesvirus proteases, whereas structural studies, show a complete active site in each monomer, away from the dimer, interface. Here we report kinetic, biophysical and crystallographic, characterizations of structure-based mutants in the dimer interface of, human cytomegalovirus (HCMV) protease. Such mutations can produce a, 1,700-fold reduction in the kcat while having minimal effects on the K(m)., Dimer stability is not affected by these mutations, suggesting that, dimerization itself is insufficient for activity. There are large changes, in monomer conformation and dimer organization of the apo S225Y mutant, enzyme. However, binding of an activated peptidomimetic inhibitor induced, a conformation remarkably similar to the wild type protease. Our studies, suggest that appropriate dimer formation may be required to indirectly, stabilize the protease oxyanion hole, revealing a novel mechanism for, dimerization to regulate enzyme activity.
+<StructureSection load='1jq6' size='340' side='right'caption='[[1jq6]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1jq6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_betaherpesvirus_5 Human betaherpesvirus 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JQ6 FirstGlance]. <br>
+</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=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</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=1jq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jq6 OCA], [https://pdbe.org/1jq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jq6 RCSB], [https://www.ebi.ac.uk/pdbsum/1jq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jq6 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SCAF_HCMVA SCAF_HCMVA] Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein UL86 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein UL86. Cleavages products are evicted from the capsid before or during DNA packaging (By similarity).  Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging (By similarity).  Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein UL86. Multimerizes in the nucleus such as protein UL86 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging (By similarity).
+== 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/jq/1jq6_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1jq6 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Biochemical studies indicate that dimerization is required for the catalytic activity of herpesvirus proteases, whereas structural studies show a complete active site in each monomer, away from the dimer interface. Here we report kinetic, biophysical and crystallographic characterizations of structure-based mutants in the dimer interface of human cytomegalovirus (HCMV) protease. Such mutations can produce a 1,700-fold reduction in the kcat while having minimal effects on the K(m). Dimer stability is not affected by these mutations, suggesting that dimerization itself is insufficient for activity. There are large changes in monomer conformation and dimer organization of the apo S225Y mutant enzyme. However, binding of an activated peptidomimetic inhibitor induced a conformation remarkably similar to the wild type protease. Our studies suggest that appropriate dimer formation may be required to indirectly stabilize the protease oxyanion hole, revealing a novel mechanism for dimerization to regulate enzyme activity.
-==About this Structure==
+Molecular mechanism for dimerization to regulate the catalytic activity of human cytomegalovirus protease.,Batra R, Khayat R, Tong L Nat Struct Biol. 2001 Sep;8(9):810-7. PMID:11524687<ref>PMID:11524687</ref>
-JQ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_5 Human herpesvirus 5]. Active as [http://en.wikipedia.org/wiki/Assemblin Assemblin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.97 3.4.21.97] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JQ6 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Molecular mechanism for dimerization to regulate the catalytic activity of human cytomegalovirus protease., Batra R, Khayat R, Tong L, Nat Struct Biol. 2001 Sep;8(9):810-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11524687 11524687]
+</div>
-[[Category: Assemblin]]
+<div class="pdbe-citations 1jq6" style="background-color:#fffaf0;"></div>
-[[Category: Human herpesvirus 5]]
-[[Category: Single protein]]
-[[Category: Batra, R.]]
-[[Category: Khayat, R.]]
-[[Category: Tong, L.]]
-[[Category: cytomegalovirus]]
-[[Category: dimerization]]
-[[Category: enzyme activity regulation]]
-[[Category: herpesvirus]]
-[[Category: serine protease]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:28:25 2007''
+==See Also==
+*[[Virus protease 3D structures|Virus protease 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Human betaherpesvirus 5]]
+[[Category: Large Structures]]
+[[Category: Batra R]]
+[[Category: Khayat R]]
+[[Category: Tong L]]

1jq6

From Proteopedia

Current revision

HUMAN CYTOMEGALOVIRUS PROTEASE DIMER-INTERFACE MUTANT, S225Y

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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